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PubMed1993

Reduction of ricin toxicity without impairing the saccharide-binding properties by chemical modification of the carboxyl groups.

The usefulness of ricin as a research tool is handicapped by its extremely biohazardous nature. In this work, ricin toxicity has been reduced by chemical modification of carboxyl groups using 1-ethyl-3(3-dimethylaminopropyl) carbodiimide and [14C]glycine methyl ester. The reaction was carried out in 8 M urea and in the presence of 0.1 M lactose to protect the groups involved in saccharide binding. Together with carboxyl groups, tyrosine residues were also modified. The maximum modification achieved was 13 carboxyl groups and 7 tyrosines per molecule (about 30% of total carboxyls and tyrosines). The modification did not alter substantially the strength and specificity of the carbohydrate-binding ability of the lectin, as observed by hemagglutination tests and by inhibition assays with different carbohydrate structures. However, the LD50 decreased 90-fold when the highest modification was achieved. Therefore, the modified lectin can be used more safely in the study of galactose-containing carbohydrates.

Animals↗
PubMed2001

Identification and location of a cysteinyl posttranslational modification in an amyloidogenic kappa1 light chain protein by electrospray ionization and matrix-assisted laser desorption/ionization mass spectrometry.

Amyloid-deposited light chain (AL) amyloidosis is correlated with the overproduction of a monoclonal immunoglobulin light chain protein by a B-lymphocyte clone. Since the amyloid fibril deposits in AL amyloidosis most often consist of the N-terminal fragments of the light chain, the majority of studies have focused on the determination of the primary structure of the protein, and reducing agents have been used routinely in the initial purification process. In this study, two light chain proteins were isolated and purified, without reduction, from the urine of a patient diagnosed with kappa 1 (kappa1) AL amyloidosis. One protein had a relative molecular mass of 12,000 and the other 24,000. Electrospray ionization and matrix-assisted laser desorption/ionization mass spectrometry, in combination with enzymatic digestions, were used to verify the amino acid sequences and identify and locate posttranslational modifications in these proteins. The 12-kDa protein was confirmed to be the N-terminal kappa1 light chain fragment (variable region) consisting of residues 1-108 or 1-109 and having one disulfide bond. The 24-kDa protein was determined to be the intact kappa1 light chain containing a cysteinyl posttranslational modification at Cys214 and disulfide bonds located at Cys23-Cys88, Cys134-Cys194, and Cys214-Cys. The methods used in this report enable high-sensitivity determination of amino acid sequence and variation in intact and truncated light chains as well as posttranslational modifications. This approach facilitates consideration of the effect of cysteinylation on the native protein structure and the potential involvement of this modification in AL amyloidosis.

Amino Acid Sequence↗
PubMed1999

Prevalence of CTGCAG recognizing restriction and modification systems in ruminal selenomonades.

Analysis of restriction and modification activities in natural population of Selenomonas ruminantium have revealed the prevalence of CTGCAG (Pst I isoschizomers) recognizing restriction and/or modification systems in these bacteria. Pst I isoschizomeric restriction endonucleases were detected in 4 out of 15 strains tested. In one strain, the Pst I isoschizomeric restriction system was accompanied by another restriction and modification system recognizing GAATTC sequence (Eco RI isoschizomer). Four other strains contained CTGCAG specific methylases which lacked cognate endo-nuclease activities. Presence of identical restriction and modification systems in both of subspecies of S. ruminantium, as well as the occurrence of Pst I isoschizomers in various combinations, indicate the possibility of horizontal transfer of genes coding for these systems.

Journal Article↗
PubMed1994

A unique antigenic determinant on collagen II closely associated with age related abnormal modification.

During aging, a variety of proteins undergo a non-enzymatic modification, such as oxidation, attachment of lipid peroxide, and glycation. In particular, the long-lived extracellular matrix proteins in connective tissue may be common targets for this kind of modification which, in turn, is involved in the pathogenesis of age related diseases. In the present study, we demonstrate that the age related modification on collagen II generates (a) new epitope(s). Furthermore, we established an immunochemical assay which is specifically suited to monitor the extent of abnormal modification of collagen II.

Adolescent↗
PubMed2003

Nonspecific depolarization of the plasma membrane potential induces cytoskeletal modifications of bovine corneal endothelial cells in culture.

Modifications in the cell membrane potential have been suggested to affect signaling mechanisms participating in diverse cellular processes, many of which involve structural cellular alterations. In order to contribute some evidence in this respect, we explored the effects of several depolarizing procedures on the structure and monolayer organization of bovine corneal endothelial cells in culture. Visually confluent cell monolayers were incubated with or without the depolarizing agent, either in a saline solution or in culture medium for up to 30 min. Membrane potential was monitored by fluorescence microscopy using oxonol V. Fluorescent probes were employed for F-actin, microtubules, and vinculin. Depolarization of the plasma membrane, achieved via the incorporation of gramicidin D into confluent endothelial cells or by modifications of the extracellular saline composition, provoked an increment of oxonol fluorescence and changes in cell morphology, consisting mainly of modifications in the cytoskeletal organization. In some areas, noticeable intercellular spaces appear. The cytoskeleton modifications mainly consist of a marked redistribution of F-actin and microtubules, with accompanying changes in vinculin localization. The results suggest that the depolarization of the plasma membrane potential may participate in mechanisms involved in cytoskeleton organization and monolayer continuity in corneal endothelial cells in culture.

Actin Cytoskeleton↗
PubMed1993

Calcium activated proteolysis and protein modification in the U18666A cataract.

Proteolytic modifications of specific water soluble lens crystallins during U18666A cataract formation in young rats were identified by two dimensional gel electrophoresis and contrasted with those produced by incubating control lens homogenates with calcium. Protein changes which began in clear precataractous lenses at 12 days age included a decrease in 31 and 27 kDa (likely to be beta B1a and beta A3, respectively) crystallin polypeptides, increase in 25 kDa basic polypeptide, appearance of new polypeptide at 30 kDa and modification of alpha A-crystallin. Further modification of both alpha- and beta-crystallins occurred as cataracts formed; they progressed from early to advanced stage within a span of 4 days. During this period polypeptides beta B1a and beta A3 almost completely disappeared and several new components of 23-26 kDa in beta-crystallin region appeared. Extensive modification of alpha A resulted in appearance of new components of less than 20 kDa. Most of the gamma-crystallins disappeared from the water soluble proteins in advanced cataract lenses of 18 day old rats presumably by leaking out of the lens. The water insoluble proteins which accumulated in the cataract were very similar to modified crystallins which appeared in the water soluble fraction. In vitro incubation of normal lens water soluble proteins with calcium duplicated most of the protein changes seen during cataract progression. Immunoblotting studies with antisera to rat alpha- and beta-crystallins revealed the identity of most of the modified water soluble proteins.(ABSTRACT TRUNCATED AT 250 WORDS)

Androstenes↗
PubMed1994

Glutathione dependent modification of bovine lens aldose reductase.

Bovine lens aldose reductase (ALR2) is readily modified by glutathione disulphide (GSSG) to an enzyme form (GS-ALR2) exhibiting a reduced catalytic efficiency with all the substrates tested and a reduced susceptibility to inhibition. The modification, which is completely reversed by reduced glutathione (GSH) or dithiothreitol occurs by a pseudo-first-order process with respect to the enzyme and a second order rate constant of 30 +/- 0.1 mol-1 min-1 at 25 degrees C was determined. By measuring the residual activity of ALR2 incubated in different glutathione redox buffers at 25 degrees C, an apparent redox equilibrium constant of 1.4 +/- 0.1 was evaluated. Thus the rate and the maximal extent of ALR2 inactivation are proportional to the redox ratio of the thiol used as modifying agent (i.e. [GSH]/[GSSG]). The stoichiometric reversibility of the enzyme modification might be impaired by a reduced solubility of GS-ALR2 with respect to ALR2 and by an increased susceptibility of the modified enzyme to proteolysis. While the native enzyme form is rather insensitive to proteolytic breakdown. GS-ALR2 is easily degraded by chymotrypsin with the generation of a peptide of 26 kDa with an aminoacid sequence at the aminoterminal side compatible with proteolysis at level of Tyr 7 of aldose reductase. A reduced efficiency in the enzyme-cofactor binding following the GSSG dependent modification of ALR2, appears to be associated to the thiol accessibility of GS-ALR2 measured at different temperatures. GS-ALR2 is characterized by the presence of one glutathione residue, linked through a mixed disulphide bond. This is sustained by: (i) the isoelectric point for the modified enzyme of 4.75, which is 0.1 pH units lower than that observed for the native enzyme, which indicates the contribution of an acidic residue to the pI of GS-ALR2; (ii) the incorporation of radioactivity coming from [3H] labelled GSSG accounting for the presence of one equivalent of glutathione per mole of enzyme. Besides being a general feature of protein reactivity in oxidative conditions, the glutathione-mediated ALR2 modification might be part of a cell strategy to preserve reducing power in conditions of oxidative stress.

Aldehyde Reductase↗
PubMed1995

Biochemical-morphological modifications of platelet membranes during pregnancy-induced hypertension.

A platelet (PLT) function modification has been reported in normal pregnancies compared with the nonpregnant condition and it has been hypothesized to play a central role in the pathogenesis of pregnancy-induced hypertension (PIH). The aims of the present study were (i) to evaluate the lipid composition, fluidity at different depths, transport functions, and ultrastructural features of the PLT membrane in PIH and (ii) to ascertain whether similar modifications may be determined by the state of pregnancy in comparison with the nonpregnant condition. The platelets of healthy pregnant women (HPW) showed: (i) an increase in Ca2+ ATPase activity, (ii) a decreased fluidity of the deeper site of the membrane, (iii) a reduced cholesterol concentration, with an increased ratio between unsaturated and saturated fatty acids; (iv) a decreased intramembranous particles (IMP) distribution factor (DF) of the plasma membrane E face in comparison with healthy nonpregnant women. When comparing women affected by PIH with HPW, we observed (i) reduced Na+/K+ ATPase activity and enhanced Ca2+ ATPase activity and intraplatelet calcium concentrations, (ii) an increased membrane fluidity, (iii) an increased cholesterol concentration and ratio between unsaturated and saturated fatty acids, (iv) a reduction of the IMP number and the DF. Pregnancy produces a deep modification of the platelet plasma membrane, and PIH produces a more pronounced alteration of the maternal platelets, which can be responsible for the observed modifications in placental blood flow and in the fetomaternal exchange.

Blood Platelets↗
PubMed1996

Two-dimensional electrophoretic analysis of compartment-specific hepatic protein charge modification induced by thioacetamide exposure in rats.

Thioacetamide (TA) is a well-known hepatotoxicant. It has been reported that an obligate intermediate of TA binds to proteins with the formation of acetylimidolysine derivatives that are responsible for TA-induced hepatotoxic effects. TA has also been reported to cause chemically induced cell death via both apoptosis and necrosis. The objective of this study was 2-fold: first, to investigate the effect of TA exposure on protein charge modifications in the rat liver and second, to study the role of these molecular correlates in the regulation of cell death. Male Sprague-Dawley rats (200-225 g, 7-8 weeks old) were divided into four major groups and treated intraperitoneally with a 12-fold dose range of TA (50, 150, 300, and 600 mg TA/kg) dissolved in water. Using whole liver extracts, alterations in the hepatic protein pattern following treatment with the 12-fold dose range of TA were studied using high-resolution, two-dimensional polyacrylamide gel electrophoresis and computerized image analysis. The results indicate that charge modification was clearly evident as early as 2 hr with the lowest dose of 50 mg TA/kg. At this dose and time endoplasmic reticulum proteins, calreticulin, grp78, and ER6O exhibited acidic charge variants. The effect of TA became more prominent with dose and time. Generally the elevation of charge modification indices (CMI) by TA appeared to reach a peak between 4 and 6 hr and then while CMI either leveled off or declined in the lower two doses of 50 and 150 mg TA/kg, it continued to remain elevated with the higher doses of 300 and 600 mg TA/kg. This dichotomy in the elevation of CMI is in close correspondence to the pattern of cell death observed with a similar dose range of TA, where lower doses (50 and 150 mg TA/kg) predominantly cause cell death via apoptosis while higher doses cause cell death via necrosis. Delayed charge modification was observed with the cytosolic hsc70s with the 300 and 600 mg TA/kg treatments, indicating that the reactive metabolite(s) slowly leak out into the cytosol from the endoplasmic reticulum. There were no alterations in the mitochondrial proteins hsp60 and grp75, suggesting that TA has no effect on the mitochondrion, its effects primarily being confined to the endoplasmic reticulum. The concept of looking at these proteins as biomarkers of tissue injury has validity. These changes may be indicators of bioactivation and adduct formation and also may be signaling events in the regulation of the mode of cell death.

Animals↗
PubMed1998

Surface Properties of Fluorosilicone Copolymers and Their Surface Modification Effects on PVC Film.

The fluorosilicone copolymers were synthesized using a fluorine-containing monomer and silicone-containing monomers by free-radical random copolymerization, and their surface properties and surface modification ability were investigated. The fluorine-containing monomer used was perfluoroalkyl ethyl acrylate (FA), and the silicone-containing monomers used were 3-[tris(trimethylsilyloxy)silyl]propyl methacrylate (SiMA), vinyltrimethoxy silane (VTMS), and vinyltriethoxy silane (VTES). The surface free energies of the fluorosilicone copolymers prepared were estimated from the contact angle data measured by sessile-drop method. And, the surface free energies of poly(vinyl chloride) (PVC) films modified by the fluorosilicone copolymers were also analyzed using the contact angle data. The fluorosilicone copolymers exhibit the surface free energies of about 8-23 dyn/cm dependent on the molecular weight of the fluorosilicone copolymers. The surface free energies of the fluorosilicone copolymers decrease with increasing molecular weight in the range of 2,000-10,000 (Mw). Among the fluorosilicone copolymers prepared in this study, PFA-r-PSiMA was found to be the most effective as a surface modification agent for PVC film. The inherent surface free energy of PFA-r-PSiMA was estimated to be about 9.0 dyn/cm. The desirable molecular weight of PFA-r-PSiMA seems to be more than 4,000 (Mw). However, it is expected that the fluorosilicone copolymers having the molecular weight of much higher than 10,000 (Mw) may not be suitable as surface modification additives because their compatibility with other polymers will decrease with the molecular weight. The optimum concentration of PFA-r-PSiMA added to PVC film is about 1.0 wt.%. PFA-r-PSiMA is expectedto be an effective additive for surface modification of PVC films. Copyright 1998 Academic Press.

Journal Article↗
PubMed2000

Adsorption and Chemical Modification of Phenols on a Silver Surface.

The adsorption of phenols of different natures on silver colloidal particles is studied here by surface-enhanced Raman spectroscopy (SERS). The studied compounds can be classified in three groups: (a) cinnamic acic derivatives: caffeic and isoferulic acids; (b) catechol; and (c) the phenols derived from benzoic acid: m- and p-hydroxybenzoic acids and salicylic, vanillic, and gallic acids. The interest of these compounds lies in the fact that they are naturally occurring molecules with significant importance in relation to plant metabolism, soil chemistry, and vegetal food stability. In addition, many of these compounds have antioxidant properties derived from their high affinity toward atmospheric oxygen. They exhibit high reactivity that may be enhanced in the presence of a metal surface such as those employed for SERS spectroscopy. From the SERS results it can be deduced that a clear chemical change of caffeic and gallic acid and catechol occurred. The chemical modification consists mainly of polymerization connected to existence in the molecule of o-diphenol moieties. In the case of m-hydroxybenzoic acid the chemical change may occur at low pH at which a reorientation of the molecule on the surface takes place, while in the o-hydroxybenzoic acid the only chemical change seems to be the internal H bond breakdown induced by the complexation with the metal. Finally, isoferulic and p-hydroxybenzoic acids do not show any chemical modification upon adsorption on the metal, which takes place through the carboxylate group adopting the molecule a standing up orientation. The case of vanillic acid is not so clear, although possible chemical modification is also possible for this adsorbate. From the results found in this work it can be inferred that the factors influencing possible chemical modification are the chemical structure of the adsorbate and its orientation and interaction with the surface. Copyright 2000 Academic Press.

Journal Article↗
PubMed1998

The hydrophobic domains in the carboxyl-terminal signal for GPI modification and in the amino-terminal leader peptide have similar structural requirements.

Proteins having a glycosyl-phosphatidylinositol (GPI) membrane anchor are synthesized with a carboxyl-terminal signal that is cleaved in the endoplasmic reticulum prior to GPI modification. The signal is characterized by a moderately hydrophobic domain downstream from the cleavage/modification site. The essential features of this domain were characterized using a truncated version of folate receptor (FR) type beta (FR-beta delta 5) in which its five carboxyl-terminal amino acid residues were deleted without affecting the efficiency of GPI modification. The amino acids at various positions in the hydrophobic domain were systematically altered and the extent of GPI modification of the recombinant proteins was determined by measuring [3H]folic acid binding at the cell surface, by Western blot analysis and from the sensitivity of the proteins to phosphatidylinositol-specific phospholipase C (PI-PLC). The results indicate that a threshold level of hydrophobicity exists at a single position below which the efficiency of GPI modification decreases with increasing hydrophilicity. Further, the hydrophobic domain is characterized by a hydrophobicity profile and not merely a minimum overall hydrophobicity. Thus, a leucine-rich core hydrophobic segment of six to eight amino acid residues is more sensitive to relatively small hydrophilic substitutions compared to its flanking regions and such mutations could be compensated by a hydrophobic substitution elsewhere within this core segment. Such a hydrophobicity profile is characteristic of the amino-terminal leader peptide. When the entire hydrophobic domain of the leader peptide of FR-beta (12 amino acid residues) was substituted with the hydrophobic domain of the GPI signal (13 amino acids), it was possible to obtain expression of FR-beta on the cell surface. In this construct, point mutations in the core hydrophobic segment and in the flanking regions within the substituting peptide produced a similar pattern of effects on the cell surface receptor expression compared to the corresponding mutations in the GPI signal of FR-beta. The results suggest that common principles may govern interactions of the hydrophobic domains of the GPI signal and the leader peptide with the endoplasmic reticulum.

Amino Acid Sequence↗
PubMed1999

Recognition of the carboxyl-terminal signal for GPI modification requires translocation of its hydrophobic domain across the ER membrane.

A carboxyl-terminal hydrophobic domain is an essential component of the processed signal for attachment of the glycosyl-phosphatidylinositol (GPI) membrane anchor to proteins and it is linked to the site (omega) of GPI modification by a spacer domain. This study was designed to test the hypothesis that the hydrophobic domain interacts with the lipid bilayer of the endoplasmic reticulum (ER) membrane to optimally position the omega site for GPI modification. The hydrophobic domain of the GPI signal in the human folate receptor (FR) type alpha was substituted with the carboxyl-terminal segment of the low-density lipoprotein receptor (LDLR), including its membrane spanning region, without altering either the spacer or the omega site. The FR-alpha/LDLR chimera was not GPI modified but was attached to the plasma membrane by a polypeptide anchor. When the carboxyl-terminal half of the hydrophobic transmembrane polypeptide in the FR-alpha/LDLR chimera was altered by introduction of negatively charged (Asp) residues, or when the cytosolic domain in the chimera was deleted, the mutated proteins became GPI-anchored. On the other hand, attachment of a carboxyl-terminal segment of LDLR including the entire cytosolic domain to FR-alpha converted it into a transmembrane protein. The results indicate that in the FR-alpha/LDLR chimera the inability of the cellular machinery for GPI modification to recognize the hydrophobic domain is not due to the intrinsic nature of the peptide, but is rather due to the retention of the peptide within the lipid bilayer. It follows that the hydrophobic domain in the signal for GPI modification must traverse the ER membrane prior to recognition of the omega site by the GPI-protein transamidase. The results thus establish a critical topographical requirement for recognition of the GPI signal in the ER.

Amino Acid Sequence↗
PubMed1999

The effect of physician office visits on CHD risk factor modification as part of a worksite cholesterol screening program.

BACKGROUND: Elevated serum cholesterol is a major risk factor for CHD. Primary prevention through behavioral modification has been designated first-line treatment for patients with elevated cholesterol. In this study, we assessed the impact of a physician office visit after a worksite cholesterol screening on self-reported changes in diet, weight loss, exercise, and smoking. We hypothesized that those individuals who had a physician office visit regarding cholesterol would make more changes in CHD risk factors than those who did not have such a visit. METHODS: A cohort of 4,928 participants from 33 work-sites in Massachusetts and Rhode Island had baseline CHD risk factors evaluated at a cholesterol screening and 4,473 were available at follow-up 6 months later by telephone interview. A total of 1,957 had elevated cholesterol levels (>/=200 mg;/dl) and were instructed to visit their physician, in addition to receiving educational materials related to CHD risk factor modification. RESULTS: Most individuals with elevated cholesterol levels had other prevalent self-reported CHD risk factors at baseline: 58% consumed high-fat diets (>30% fat), 43% were overweight, 60% had a sedentary lifestyle (sweat-related physical activity <3 x per week), and 22% were cigarette smokers. After 6 months of follow-up, 74% of participants with high-fat diets reported eating a lower fat diet, 71% of overweight participants reported weight loss, 53% of sedentary participants attempted to increase physical activity, and 38% of smokers decreased or quit cigarette smoking. Thirty-five percent of participants completed the referral for a physician office visit to discuss their elevated cholesterol determined at the baseline worksite screening. However, these individuals showed only a modest change (which was not statistically significant) in self-reported CHD risk factors compared with those who did not have follow-up physician visits after adjusting for age, sex, race, education, occupation, medical insurance, time since last doctor visit, diabetes, and hypertension. Objective measurements of serum cholesterol, body mass index, and dietary score were likewise modestly improved and not statistically significant. CONCLUSIONS: In 6 months of follow-up, high absolute levels of CHD risk factor modification were observed after a worksite cholesterol screening. A physician office visit added only a modest but not statistically significant benefit for further CHD risk factor modification. These findings indicate that the follow-up cholesterol-related physician visit had little added clinical benefit over the screening intervention alone.

Adult↗
PubMed1979

Control of acetyl-CoA carboxylase by covalent modification.

In this review, various experiments which establish the occurrence of covalent modification mechanisms, both in vivo and in vitro, in the control of acetyl-CoA carboxylase have been presented. It is interesting to note that phosphorylation of the carboxylase results in disaggregation of the active species. These studies indicate that aggregation and disaggregation of the enzyme are involved in the control of carboxylase activity. Our covalent modification mechanism and the allosteric control mechanism share a common ground in that both mechanisms affect the equilibrium between protomers and polymers of the enzyme. However, it is clear that the allosteric control mechanism cannot function alone under normal physiological conditions. Covalent modification of the carboxylase is prerequisite for efficient functioning of the allosteric mechanism. There are many aspects of the regulation of acetyl-CoA carboxylase which require further clarification. However, it is now established that short-term control of acetyl-CoA carboxylase involves the covalent modification mechanism.

Acetyl-CoA Carboxylase↗
PubMed1975

In vitro modification and restriction of phage phi-105c DNA with Bacillus subtilis N cell-free extract.

The enzymes involved in host-controlled modification and restriction by Bacillus subtilis strain N were detected in cell free extracts. In the presenct of Mg2+ the N-specific endonucleases cleaved unmodified DNA but did not attack phi-105C. N DNA carrying N-specific modification. The restriction endonuclease required neither SAM nor ATP for its activity. The N-specific modification enzyme was active only in the presence of SAM, indicating that modification in this syteem is a methylation of DNA.

Adenosine Triphosphate↗
PubMed1980

A new hypothesis for synaptic modification: an interactive process between postsynaptic competition and presynaptic regulation.

Based on recent physiological observations, a new hypothesis for the algorithm for synaptic modification is proposed: an interactive process between postsynaptic competition and presynaptic regulation controls the synaptic modification, and both functions obey the same competitive rule. A fundamental algorithm for the competitive rule is proposed and analysed. The interactive process is deomposed into two procedures. The first one is a postsynaptic competition, in which all synapses making contact with the same postsynaptic cell compete for their terminal sites, and the postsynaptic cell makes demands for synaptic modification upon the presynaptic cells. The second one is a presynaptic regulation, in which the presynaptic cell regulates the postsynaptic demands and determines the net amount of the modification for each snyapse originating from it. The performance of the alforithm has been simulated on a digital computer. The initial structure of the simulated neural network consists of randomly-connected presynaptic and postsynaptic cells, with no other structures assumed. After repetitive presentations of a uniform stimulus, the basic configurations of neural connections (one-to-one, one-to-many, many-to-one and many-to-many connections) are organized in dependence on the parameters of the algorithm.

Axonal Transport↗
PubMed1979

Host-controlled modification and restriction in Bacillus subtilis: Bsu 168-system and BsuR-system in B. subtilis 168.

A Bsu168-specific restriction deficient (r168-) mutant of Bacillus subtilis Marburg 168 was transformed to be BsuR-specific restriction proficient (rR+) with B. subtilis R DNA as efficiently as the Bsu 168-specific restriction proficient (r168+) parental strain (hsrM+, hsdR-). We constructed rR+ mR+ r168+ m168+ strain (ISMR 4), rR+ mR+ r168- m168+ strain (ISR 11) and rR+ mR+ r168- m168- strain (ISR 6) from strain 101 (r168+ m168+), strain 1012 (r168- m168+) and strain RM125 (r168- m168-), respectively by transformation with B. subtilis R DNA, and tested their restriction and modification activities on phage phi 105C. The results show that the sites recognized by Bsu168-specific restriction and modification enzymes and the sites recognized by BsuR-specific ones are not overlapping. We conclude that the Bsu168-modification and restriction system and the BsuR-modification and restriction system are controlled independently by two distinct sets of genes in the rR+ mR+ transformant of r168+ m168+ strain B. subtilis 168.

Bacillus subtilis↗