Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “TAILS”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 811 records · Page 45Linked to original sources
PubMed2001

The nonhelical tail domain of keratin 14 promotes filament bundling and enhances the mechanical properties of keratin intermediate filaments in vitro.

Keratin filaments arise from the copolymerization of type I and II sequences, and form a pancytoplasmic network that provides vital mechanical support to epithelial cells. Keratins 5 and 14 are expressed as a pair in basal cells of stratified epithelia, where they occur as bundled arrays of filaments. In vitro, bundles of K5-K14 filaments can be induced in the absence of cross-linkers, and exhibit enhanced resistance to mechanical strain. This property is not exhibited by copolymers of K5 and tailless K14, in which the nonhelical tail domain has been removed, or copolymers of K5 and K19, a type I keratin featuring a short tail domain. The purified K14 tail domain binds keratin filaments in vitro with specificity (kD approximately 2 microM). When transiently expressed in cultured cells, the K14 tail domain associates with endogenous keratin filaments. Utilization of the K14 tail domain as a bait in a yeast two-hybrid screen pulls out type I keratin sequences from a skin cDNA library. These data suggest that the tail domain of K14 contributes to the ability of K5-K14 filaments to self-organize into large bundles showing enhanced mechanical resilience in vitro.

Animals↗
PubMed2002

Interference with the cytoplasmic tail of gp210 disrupts "close apposition" of nuclear membranes and blocks nuclear pore dilation.

We tested the hypothesis that gp210, an integral membrane protein of nuclear pore complexes (NPCs), mediates nuclear pore formation. Gp210 has a large lumenal domain and small COOH-terminal tail exposed to the cytoplasm. We studied the exposed tail. We added recombinant tail polypeptides to Xenopus nuclear assembly extracts, or inhibited endogenous gp210 tails using anti-tail antibodies. Both strategies had no effect on the formation of fused flattened nuclear membranes, but blocked NPC assembly and nuclear growth. Inhibited nuclei accumulated gp210 and some nucleoporin p62, but failed to incorporate nup214/CAN, nup153, or nup98 and were defective for nuclear import of lamin B3. Scanning and transmission EM revealed a lack of "closely apposed" inner and outer membranes, and the accumulation of novel arrested structures including "mini-pores." We conclude that gp210 has early roles in nuclear pore formation, and that pore dilation is mediated by gp210 and its tail-binding partner(s). We propose that membrane fusion and pore dilation are coupled, acting as a mechanism to control nuclear pore size.

Amino Acid Sequence↗
PubMed2000

Clinical effectiveness of new stent design: randomized single-blind comparison of tail and double-pigtail stents.

BACKGROUND AND PURPOSE: Stent morbidity appears to be secondary to lower urinary tract irritation. In an effort to decrease stent morbidity, a "one size fits all" Tail stent (Microvasive [Boston Scientific] Natick, MA) was developed with a 7F proximal pigtail and 7F shaft which tapers to a lumenless straight 3F tail. PATIENTS AND METHODS: We randomized 60 patients in a single-blind fashion to a 7F tail stent or 7F double-pigtail Percuflex stent. Patients were evaluated at the time of stent removal and 2 weeks later with a standardized questionnaire assessing: irritative lower tract symptoms individually and on a total scale of 0 (no symptoms) to 30 (worst symptoms), obstructive lower tract symptoms (on a total scale of 0-20), and upper tract irritative symptoms (on a total scale of 0-10). RESULTS: Patient age, weight, and height were similar in the two groups. Complications, including fever, urinary tract infections, emergency room visits, and the need for antispasmodics and pain medication, also demonstrated no significant difference. At the time of stent removal, patients who received a tail stent had significantly less urinary frequency and a statistically significant (21%) decrease in overall irritative voiding symptoms (12.2 v 15.4; p = 0.048). Two weeks after stent removal, the total irritative voiding symptoms was markedly decreased in both groups (7.1 in the Tail v 5.3 in the double-pigtail group; p = 0.15). Obstructive bladder and flank symptoms were not significantly different in the two stent groups, either at the time of stent removal or at 2 weeks after removal. CONCLUSION: In this randomized, single-blind study, the 7F Tail stent produced significantly less irritative symptoms than did the standard 7F double-pigtail stent. Obstructive symptoms tended to be less with the new stent, while flank symptoms were similar.

Adult↗
PubMed1990

Endocytosis via coated pits mediated by glycoprotein receptor in which the cytoplasmic tail is replaced by unrelated sequences.

Rat 6 fibroblast cell lines expressing wild-type chicken liver glycoprotein receptor (CHL) or chimeric receptors with alternate cytoplasmic tails were produced to study the role of the cytoplasmic tail in mediating receptor localization in coated pits and endocytosis of ligand. Cells expressing CHL or cells expressing a hybrid receptor that contains the cytoplasmic tail of the asialoglycoprotein receptor display high-efficiency endocytosis of N-acetylglucosamine-conjugated bovine serum albumin in experiments designed to measure an initial internalization step, as well as in studies of continuous uptake and degradation. Substitution of the cytoplasmic tail by the equivalent domain of rat Na,K-ATPase beta subunit or by a stretch of Xenopus laevis globin beta chain does not abolish endocytosis but decreases the endocytosis rate constant from 15%-16%/min to 2.4% and 6.5%/min, respectively. Electron microscopy was used to visualize the glycoprotein binding sites at the surface of Rat 6 cells transfected with the various receptors. The percentage of receptors found in coated areas ranged from 32% for CHL to 9% for the Na,K-ATPase hybrid, indicating that clustering in coated pits correlates with efficiency of endocytosis. We concluded that replacement of the CHL cytoplasmic tail with unrelated sequences does not prevent, but decreases to varying extents, coated-pit localization and endocytosis efficiency. The construct with NH2-terminal globin tail lacks a signal for high-efficiency localization in coated pits but nevertheless is directed to the pits by an alternative mechanism.

Amino Acid Sequence↗
PubMed1992

Mutation of a tyrosine localization signal in the cytosolic tail of yeast Kex2 protease disrupts Golgi retention and results in default transport to the vacuole.

Kex2 protease processes pro-alpha-factor in a late Golgi compartment in Saccharomyces cerevisiae. The first approximately 30 residues of the 115 amino acid CO2H-terminal cytosolic tail (C-tail) of the Kex2 protein (Kex2p) contain a Golgi retention signal that resembles coated-pit localization signals in mammalian cell surface receptors. Mutation of one (Tyr713) of two tyrosine residues in the C-tail or deletion of sequences adjacent to Tyr713 results in loss of normal Golgi localization. Surprisingly, loss of the Golgi retention signal resulted in transport of C-tail mutant Kex2p to the vacuole (yeast lysosome), as judged by kinetics of degradation and by indirect immunofluorescence. Analysis of the loss of Kex2 function in vivo after shutting off expression of wild-type or mutant forms proved that mutations that cause rapid vacuolar turnover do so by increasing the rate of exit of the enzyme from the pro-alpha-factor processing compartment. The most likely explanation for these results is that mutation of the Golgi retention signal in the C-tail results in transport of Kex2p to the vacuole by default. Wild-type Kex2p also was transported to the vacuole at an increased rate when overproduced, although apparently not due to saturation of a Golgi-retention mechanism. Instead, the wild-type and C-tail mutant forms of Kex2p may follow distinct paths to the vacuole.

Amino Acid Sequence↗
PubMed1999

Gap junction proteins connexin32 and connexin43 partially acquire growth-suppressive function in HeLa cells by deletion of their C-terminal tails.

Our laboratory has previously reported that transfection of a connexin26 (Cx26) gene, but not connexin40 nor connexin43 (Cx43), into HeLa cells expressing no detectable level of connexins suppressed the tumorigenic phenotype of the HeLa cells both in vitro and in vivo, although all of these connexins induced gap junctional intercellular communication in HeLa cells to a similar extent. The most remarkable structural difference between connexin proteins is the length of the C-terminal cytoplasmic tail, Cx26 having almost no tail, while Cx43 and connexin32 (Cx32) have long and intermediate ones, respectively. When Cx32 and Cx43 lose their C-terminal tails, they seem to resemble Cx26 in structure. To examine whether such truncated connexins become tumor suppressive in HeLa cells, we introduced a stop codon into each of the Cx32 and Cx43 cDNAs to remove their C-terminal tails and transfected these constructs (DeltaCx) into HeLa cells. Both DeltaCx cDNAs induced GJIC as efficiently as the wild-type counterparts. Although none of the truncated connexins affected proliferation rate, the truncated Cx32 and Cx43 proteins suppressed anchorage-independent cell growth in soft agar. Furthermore, when the transfectants were injected into the backs of nude mice, tumor appearance was delayed by 7 days in animals given cells expressing truncated connexins, i.e. tumors became detectable on days 11 and 18 after injection of vector and DeltaCx transfectants, respectively. Although throughout these experiments the truncated connexins did not completely eliminate the tumorigenicity of HeLa cells, as Cx26 did, it was evident that deletion of the C-terminal tails gave both Cx32 and Cx43 a capacity for negative growth control, suggesting that the C-terminal tails of these two connexins function as a regulatory region for connexin-mediated growth control in HeLa cells.

Animals↗
PubMed1994

Mutational analysis defines a C-terminal tail domain of RAP1 essential for Telomeric silencing in Saccharomyces cerevisiae.

Alleles specifically defective in telomeric silencing were generated by in vitro mutagenesis of the yeast RAP1 gene. The most severe phenotypes occur with three mutations in the C-terminal 28 amino acids. Two of the alleles are nonsense mutations resulting in truncated repressor/activator protein 1 (RAP1) species lacking the C-terminal 25-28 amino acids; the third allele is a missense mutation within this region. These alleles define a novel 28-amino acid region, termed the C-terminal tail domain, that is essential for telomeric and HML silencing. Using site-directed mutagenesis, an 8-amino acid region (amino acids 818-825) that is essential for telomeric silencing has been localized within this domain. Further characterization of these alleles has indicated that the C-terminal tail domain also plays a role in telomere size control. The function of the C-terminal tail in telomere maintenance is not mediated through the RAP1 interacting factor RIF1: rap1 alleles defective in both the C-terminal tail and RIF1 interaction domains have additive effects on telomere length. Overproduction of SIR3, a dose-dependent enhancer of telomeric silencing, suppresses the telomeric silencing, but not length, phenotypes of a subset of C-terminal tail alleles. In contrast, an allele that truncates the terminal 28 amino acids of RAP1 is refractory to SIR3 overproduction. These results indicate that the C-terminal tail domain is required for SIR3-dependent enhancement of telomeric silencing. These data also suggest a distinct set of C-terminal requirements for telomere size control and telomeric silencing.

Alleles↗
PubMed1999

Deletions of the heavy neurofilament subunit tail in amyotrophic lateral sclerosis.

Amyotrophic lateral sclerosis (ALS) is a progressive motor neuron degeneration resulting in paralysis and death, usually within 3 years of onset. Pathological and animal studies implicate neurofilament involvement in ALS, but whether this is primary or secondary is not clear. The heavy neurofilament subunit (NFH) tail is composed of a repeating amino acid motif, usually X-lysine-serine-proline-Y-lysine (XKSPYK), where X is a single amino acid and Y is one to three amino acids. There are two common polymorphic variants of 44 or 45 repeats. The tail probably regulates axonal calibre, with interfilament spacing determined by phosphorylation of the KSP motifs. A previous study suggested an association between sporadic cases of ALS and NFH tail deletions, but two subsequent studies have found none. We have analysed samples from two different populations (UK 207, Scandinavia 323) with age-matched controls for each group (UK 219, Scandinavia 228) and have found four novel NFH tail deletions, each involving a whole motif. These were found in three patients with sporadic ALS and a family with autosomal dominant ALS, although another was also found in two young controls. In all cases motif deletions were only associated with disease when paired with the long NFH allele. The deletions all occurred within a small region of the NFH tail. This has allowed us to propose a structural organization of the tail as well as allowing observed deletions both from this study and previous reports to be organized into logical groups. These results strongly suggest that NFH motif deletions can be a primary event in ALS but that they are not common.

Adult↗
PubMed2003

The MHC class II beta chain cytoplasmic tail overcomes the invariant chain p35-encoded endoplasmic reticulum retention signal.

The human-specific p35 isoform of the invariant chain (Ii) includes an R-X-R endoplasmic reticulum (ER) retention motif that is inactivated upon HLA-DR binding. Although the masking is assumed to involve the cytoplasmic tails of class II molecules, the mechanism underlying this function remains to be investigated. Moreover, in light of the polymorphic nature of the class II cytosolic tails, little is known about the capacity of various isotypes or alleles to overcome the retention signal of Iip35. To gain further insights into these issues, we first addressed the proposed role of the HLA-DR cytoplasmic tails. As shown by flow cytometry, the presence of Iip35 in transfected HeLa cells prevented surface expression of HLA-DR molecules lacking their cytoplasmic tails (DRalphaTM/betaTM). These truncated class II molecules and Iip35 accumulated in the ER, and co-localized with calnexin, as determined by confocal microscopy. Sensitivity of DRalphaTM/betaTM to endoglycosidase H treatment confirmed that these molecules do not reach the trans-Golgi network when associated with Iip35. Further characterization revealed that the beta chain cytosolic tail is critical for efficient ER egress of class II/Iip35 complexes. Interestingly, our results clearly demonstrate for the first time that DP and DQ isotypes can also overcome the retention motif of Iip35 through a mechanism involving their very distinctive polymorphic beta chain cytoplasmic tails. Altogether, these results further dissect the masking of di-basic retention signals, and emphasize the interplay between class II molecules and Ii for the transport of the complex to the endocytic pathway.

Amino Acid Sequence↗
PubMed1995

Dietary methionine does not reduce penetrance in curly tail mice but causes a phenotype-specific decrease in embryonic growth.

The mouse mutation, curly tail, has incomplete penetrance and variable expression. Approximately 60% of the mice have a curly tail (CT), from which up to 20% may have lumbosacral spina bifida. Approximately 40% are normal, with a straight tail (ST). We tested whether L-methionine, which reduces the penetrance of neural tube defects in the Axd mouse mutant, has beneficial effects in the curly tail mutant. A single injection of L-methionine (200-1600 mg/kg body wt) on d 9 of pregnancy had no effect on the embryos, whereas there was a minor increase in penetrance at the highest dose. Chronic supplementation of L-methionine via the drinking water (1554 mg.kg body wt-1.d-1) did not shift penetrance. However, it decreased the weight of d 13 embryos from ST dams but not of those from CT dams. This phenotype-specific difference in response was evident and most unexpected. Mice from curly tail and other inbred strains were subjected to an L-methionine loading test and serum homocysteine assay. The different strains varied in their basal serum homocysteine concentrations, and they had proportionate significant increases after L-methionine loading. In CT and ST mice, basal serum homocysteine concentrations as well as the levels after loading were similar to each other and intermediate in the range of the mice tested. We conclude that L-methionine does not reduce penetrance in the curly tail mouse and that this strain reflects no derangement in L-methionine handling.

Animals↗
PubMed1998

Reduced glucose consumption in the curly tail mouse does not initiate the pathogenesis leading to spinal neural tube defects.

At embryonic stages of neural tube closure, the mouse embryo exhibits a high rate of glycolysis with glucose as the main energy source. In the curly tail mouse, often used as model system for study of human neural tube defects, a delay in closure of the posterior neuropore (PNP) is proposed to be indirectly caused by a proliferation defect in the caudal region. Because glucose is important for proliferation, we tested glucose uptake in curly tail and control embryos, and in a BALB/c-curly tail recombinant strain. The structure and expression of Glut-1, a glucose transporter molecule that is abundantly present during those embryonic stages and that has been mapped in the region of the major curly tail gene, were also studied; however, no strain differences could be demonstrated. Glucose uptake was determined by measuring glucose depletion from the medium in long-term embryo cultures that encompassed the stages of PNP closure and by measuring accumulation of 3H-deoxyglucose in short-term cultures at the stages of early and final PNP closure. Both approaches indicated a reduced glucose uptake by curly tail and recombinant embryos. Surprisingly, the uptake per cell appeared normal, accompanied by a significantly lower DNA content of the mutant embryos. Therefore, it is unlikely that reduced cell proliferation is caused by a reduction in glucose supply during the pathogenesis of the defects in curly tail embryos. The reduced DNA content as well as the reduced glucose uptake per embryo are likely downstream effects of the aberrant proliferation pattern.

Animals↗
PubMed2003

Variant of perivitelline membrane glycoprotein ZPC of Japanese quail (Coturnix japonica) lacking its cytoplasmic tail exhibits the retention in the endoplasmic reticulum of Chinese hamster ovary (CHO-K1) cells.

Avian perivitelline membrane, an investment homologous to the mammalian zona pellucida, is composed of at least two glycoproteins. Our previous studies demonstrated that one of its components, ZPC, which is synthesized in the ovarian granulosa cells, is secreted after carboxy-terminal proteolytic processing, and this event is a prerequisite event for ZPC secretion in quail. In the present study, we examined the role of the cytoplasmic tail, which is successfully removed after proteolytic processing, in membrane transport, proteolytic processing, and the secretion of quail ZPC. In pursuit of this, we produced a truncated ZPC mutant lacking the cytoplasmic tail located in its C-terminus and examined its expression in the mammalian cell line. Western blot analyses demonstrated that the cytoplasmic tail-deficient ZPC was neither secreted nor underwent proteolytic processing in the cells. Immunofluorescence analysis and the acquisition of resistance to endoglycosidase H digestion of the cytoplasmic tail-deficient ZPC demonstrated that the deletion of the cytoplasmic tail interferes with the intracellular trafficking of the protein from the endoplasmic reticulum to the Golgi apparatus. These results indicate that the cytoplasmic tail of quail ZPC might possess the determinant responsible for the efficient transport of the newly synthesized ZPC from the endoplasmic reticulum to the Golgi apparatus.

Animals↗
PubMed1987

Radium-226 contents and Rn emanation coefficients of particle-size fractions of alkaline, acid and mixed U mill tailings.

Alkaline circuit and mixed, acid and alkaline circuit U mill tailings sampled at an inactive mill site near Monticello, UT, and tailings from an active, acid-leach U mill were separated into particle-size fractions ranging from +10 mesh to -325 mesh by dry and wet separation techniques. The 226Ra contents and 222Rn emanation coefficients of these fractions were determined. Dry tailings show a high degree of aggregation that tends to mask the relation of properties, such as Ra content and Rn emanating power, to dispersed-particle size. Coarse-tailings fractions (+325 mesh) had emanation coefficients which were from 25 to 45% lower than those of their fine-fraction counterparts. Emanation coefficients measured for tailings derived from a salt roast/carbonate-leach process suggest that such are roasting does not lead to reductions in Rn emanation in the tailings derived therefrom.

Hydrogen-Ion Concentration↗
PubMed1990

Ground distribution patterns of selected radioactive, chemical, and physical contaminants from dispersion of U mill tailings.

Ground concentrations of 226Ra and total alpha activity as a function of soil depth and distance from an acidic U mill tailings pile were measured, as well as soil pH, sulfate, chloride, and conductivity. Contamination decreased with increasing soil depth and distance from the source. Most of the measured parameters were indistinguishable from background after a distance of 3.3 km from the tailings impoundment. The highest concentrations of all contaminants were contained in the particles less than 0.045 mm in diameter at the soil surface (0-0.6 cm). This fraction represents only 4% to 10% of the total soil mass. Surface soil particles greater than 2.0 mm contained higher concentrations of all contaminants than the intermediate-size (0.045-2.0 mm) fraction. Aggregate formation of the greater than 2.0-mm fraction from small particles or preferential erosion and transport of the tailings sand fractions were proposed as possible explanations. The significant correlations between various measurements were soil 226Ra vs. total alpha activity, sulfate concentration, and conductivity. The latter two parameters are indicative of sulfuric acid leached tailings. The sulfate concentration appeared to be a sensitive and easily measured indicator of tailings contamination and migration into the soil profile. Furthermore, sulfate may be used to delineate acidic U tailings from other sources of contamination (U ore dust, yellowcake, naturally elevated U and Ra) in the environment. Actual site measurements for surface 226Ra concentration were approximately twice the MILDOS computer code prediction.

Chlorides↗
PubMed1997

Arterial morphology and blood volumes of rats following 10-14 weeks of tail suspension.

We hypothesized that the structure of systemic arteries would be altered following 10-14 wk of hindlimb unloading (tail suspension) in female Sprague-Dawley rats. Tail suspension resulted in atrophy of the soleus muscle (P < or = 0.01) but no significant differences in the mass of the extensor digitorum muscle, heart, or adrenal glands. In anesthetized rats, there was no difference between groups in arterial pressure (approximately 60 mm Hg). The corresponding maximal (topical papaverine) external diameter (ED) of femoral arteries (N = 5 per group) was reduced (P < or = 0.05) in tail suspended (TS, 511 +/- 47 microm, mean +/- SD) compared with cage sedentary (CS, 615 +/- 89 microm) and food restricted weight-paired (FR, 643 +/- 61 microm) groups. Neither hematocrit, red cell, plasma, nor total blood volume differed among groups. Following systemic vasodilation with papaverine, progressive arterial inflation with liquid silicon rubber (Microfil) revealed a reduction in both ED and distensibility of the femoral artery (P < or = 0.05). To determine the effects of tail suspension on systemic arterial morphology, the vasculature of additional rats was perfusion fixed at 80 mm Hg during vasodilation. Cross sections (thickness, 8 microm) of the carotid, axillary, iliac, and femoral arteries were then evaluated. Whereas the internal diameter of femoral arteries was smaller in TS than in CS (P < 0.05), no differences were observed for other vessels among groups. Further, arterial wall thickness increased systemically (overall, P < 0.05; carotid, 24%, P < 0.01; femoral, 28%, P < 0.01) following tail suspension. These findings illustrate adaptation in the structure of conduit arteries to prolonged tail suspension, with diameter altered regionally and wall thickness increased systemically. We suggest that chronic changes in activity patterns can influence arterial structure.

Analysis of Variance↗
PubMed1998

Roles of vaccinia virus EEV-specific proteins in intracellular actin tail formation and low pH-induced cell-cell fusion.

During vaccinia virus (VV) morphogenesis intracellular mature virus (IMV) is wrapped by two additional membranes to form intracellular enveloped virus (IEV). IEV particles can nucleate the formation of actin tails which aid movement of IEVs to the cell surface where the outer IEV membrane fuses with the plasma membrane forming cell-associated enveloped virus (CEV) which remains attached to the cell, or extracellular enveloped virus (EEV) which is shed from the cell. In this report, we have used a collection of VV mutants lacking individual EEV-specific proteins to compare the roles of these proteins in the formation of IEV and IEV-associated actin tails and fusion of infected cells after a low pH shock. Data presented here show that p45-50 (A36R) is not required for IEV formation or for acid-induced cell-cell fusion, but is required for formation of IEV-associated actin tails. In contrast, gp86 (A56R), the virus haemagglutinin, is not required for formation of either IEV or IEV-associated actin tails. Data presented also confirm that p37 (gene F13L), gp42 (B5R) and gp22-24 (A34R) are needed for formation of IEV-associated actin tails and for cell-cell fusion after low pH shock. The phenotypes of these mutants were not affected by the host cell type as similar results were obtained in a range of different cells. Lastly, comparisons of the phenotypes of VV strains Western Reserve, deltaA34R and deltaA36R demonstrate that actin tails are not required for low pH-induced cell-cell fusion.

Actins↗
PubMed1999

The cytoplasmic tail of the influenza C virus glycoprotein HEF negatively affects transport to the cell surface.

The surface glycoprotein, HEF, of influenza C virus (C/Johannesburg/1/66) has been shown to undergo a post-translation conformational change that is evident in a dramatic change of electrophoretic mobility. If the corresponding gene is expressed in the absence of other viral proteins, this folding process does not occur at all or only very inefficiently. A chimaeric protein, HEF-HA(Tail), in which the short cytoplasmic tail (Arg-Thr-Lys) of HEF was replaced by the cytoplasmic tail of the haemagglutinin of an influenza A virus (fowl plague virus) was constructed. In contrast to the wild-type protein, the chimaeric protein was detected on the cell surface. No further improvement of the surface expression was observed when both the transmembrane domain and the cytoplasmic tail were replaced by the corresponding domains of either the influenza A haemagglutinin or gp40, an endogenous protein of MDCK cells. For the HEF-HA(Tail) construct this study shows that a substantial amount of the protein is converted to the 100 kDa mature form that is observed in virus-infected cells. The HEF-HA expressed on the cell surface reacted positively in esterase and haemadsorption assays, indicating that it was present in a biologically active form. The results show that the short cytoplasmic tail of HEF has a negative effect on the folding and surface transport of this protein. How this effect may be prevented during a virus infection is discussed.

Amino Acid Sequence↗
PubMed2006

RNA 3'-tail synthesis in Streptomyces: in vitro and in vivo activities of RNase PH, the SCO3896 gene product and polynucleotide phosphorylase.

As in other bacteria, 3'-tails are added post-transcriptionally to Streptomyces coelicolor RNA. These tails are heteropolymeric, and although there are several candidates, the enzyme responsible for their synthesis has not been definitively identified. This paper reports on three candidates for this role. First, it is confirmed that the product of S. coelicolor gene SCO3896, although it bears significant sequence similarity to Escherichia coli poly(A) polymerase I, is a tRNA nucleotidyltransferase, not a poly(A) polymerase. It is further shown that SCO2904 encodes an RNase PH homologue that possesses the polymerization and phosphorolysis activities expected for enzymes of that family. S. coelicolor RNase PH can add poly(A) tails to a model RNA transcript in vitro. However, disruption of the RNase PH gene has no effect on RNA 3'-tail length or composition in S. coelicolor; thus, RNase PH does not function as the RNA 3'-polyribonucleotide polymerase [poly(A) polymerase] in that organism. These results strongly suggest that the enzyme responsible for RNA 3'-tail synthesis in S. coelicolor and other streptomycetes is polynucleotide phosphorylase (PNPase). Moreover, this study shows that both PNPase and the product of SCO3896 are essential. It is possible that the dual functions of PNPase in the synthesis and degradation of RNA 3'-tails make it indispensable in Streptomyces.

Bacterial Proteins↗