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PubMed1991

Cell-surface receptor for ecotropic murine retroviruses is a basic amino-acid transporter.

The complementary DNA sequence encoding the cell-surface receptor for ecotropic host-range murine retroviruses (ecoR) shows that it contains 622 amino acids and 14 hydrophobic potentially membrane-spanning sequences. Because this receptor occurs on many or all murine cells and is probably essential for viability of cultured fibroblasts, its normal function might be to transport an essential metabolite. We expressed ecoR in Xenopus laevis oocytes by injecting RNA transcribed from the cloned cDNA. These oocytes specifically bound the gp70 envelope glycoprotein from an ecotropic murine leukaemia virus. An inward current was recorded electrophysiologically when a mixture of amino-acids was applied: this resulted from a stereoselective, saturable uptake of lysine, arginine and ornithine; it was independent of sodium and not substantially altered by gp70. Cysteine and homoserine were also taken up, but sodium was necessary for their transport. These properties of ecoR correspond to those of the y+ amino-acid transporter. Our results demonstrate the subversion of a ubiquitous cell membrane protein, in this case a basic amino acid transporter, for use as a retroviral receptor.

Animals↗
PubMed2004

Nuclear and nucleolar localization of 18-kDa fibroblast growth factor-2 is controlled by C-terminal signals.

Members of high (22-, 22.5-, 24-, and 34-kDa) and low (18-kDa) molecular mass forms of fibroblast growth factor-2 (FGF-2) regulate cell proliferation, differentiation, and migration. FGF-2s have been previously shown to accumulate in the nucleus and nucleolus. Although high molecular weight forms of FGF-2 contain at least one nuclear localization signal (NLS) in their N-terminal extension, the 18-kDa FGF-2 does not contain a standard NLS. To determine signals controlling the nuclear and subnuclear localization of the 18-kDa FGF-2, its full-length cDNA was fused to that of green fluorescent protein (GFP). The fusion protein was primarily localized to the nucleus of COS-7 and HeLa cells and accumulated in the nucleolus. The subcellular distribution was confirmed using wild type FGF-2 and FGF-2 tagged with a FLAG epitope. A 17-amino acid sequence containing two groups of basic amino acid residues separated by eight amino acid residues directed GFP and a GFP dimer into the nucleus. We systematically mutated the basic amino acid residues in this nonclassical NLS and determined the effect on nuclear and nucleolar accumulation of 18-kDa FGF-2. Lys(119) and Arg(129) are the key amino acid residues in both nuclear and nucleolar localization, whereas Lys(128) regulates only nucleolar localization of 18-kDa FGF-2. Together, these results demonstrate that the 18-kDa FGF-2 harbors a C-terminal nonclassical bipartite NLS, a portion of which also regulates its nucleolar localization.

Amino Acid Sequence↗
PubMed2004

Linkage of amino acid variation and evolution of human immunodeficiency virus type 1 gp120 envelope glycoprotein (subtype B) with usage of the second receptor.

To clarify the relationship between the amino acid variations of the gp120 of human immunodeficiency virus type 1 (HIV-1) and the chemokine receptors that are used as the second receptor for HIV, we evaluated amino acid site variation of gp120 between the X4 strains (use CXCR4) and the R5 strains (use CCR5) from 21 sequences of subtype B. Our analysis showed that residues 306 and 322 in the V3 loop and residue 440 in the C4 region were associated with usage of the second receptor. The polymorphism at residue 440 is clearly associated with the usage of the second receptor: The amino acid at position 440 was a basic amino acid in the R5 strains, and a nonbasic and smaller amino acid in the X4 strains, while the V3 loop of the X4 strains was more basic than that of the R5 strains. This suggests that residue 440 in the C4 region, which is close to the V3 loop in the three-dimensional structure, is critical in determining which second receptor is used. Analysis of codon frequency suggests that, in almost all cases, the difference at residue 440 between basic amino acids in the R5 strains and nonbasic amino acids in the X4 strains could be due to a single nucleotide change. These findings predict that the evolutionary changes in amino acid residue 440 may be correlated with evolutionary changes in the V3 loop. One possibility is that a change in electric charge at residue 440 compensates for a change in electric charge in the V3 loop. The amino acid polymorphism at position 440 can be useful to predict the cell tropism of a strain of HIV-1 subtype B.

Amino Acid Sequence↗
PubMed1996

DRPLA gene (atrophin-1) sequence and mRNA expression in human brain.

Dentatorubral pallidoluysian atrophy (DRPLA, Smith's disease) is one of five disorders currently known to result from expansion of a CAG trinucleotide repeat encoding glutamine. The reported full length cDNA sequence encodes a serine repeat and a region of alternating acidic and basic amino acids, as well as the glutamine repeat. We now report the nucleic acid and deduced amino acid sequences of the open reading frame of this gene, obtained from a series of independently isolated and sequenced cDNA clones. Eight nucleotide differences from the originally published sequence result in a change of 34 amino acids, most prominently in the region of alternating acidic and basic residues. Northern analysis and in situ hybridization indicate that atrophin-1 mRNA is expressed in multiple brain regions. The level of mRNA expression as determined by in situ hybridization in a DRPLA-diseased brain is indistinguishable from the level observed in a matched control brain. These results indicate that the correlation between atrophin-1 expression and regions of pathology in DRPLA is at best partial, and that the expanded allele does not cause a major loss of mRNA expression. The pathology of the disorder may therefore arise from the altered structure and function of the abnormal protein.

Amino Acid Sequence↗
PubMedDate not supplied

Avian influenza virus subtypes inside and outside the live bird markets, 1993-2000: a spatial and temporal relationship.

Between 1993 and 2000, gallinaceous birds, waterfowl, and environmental specimens from the live bird markets (LBMs) of the northeastern United States and non-LBM premises were tested for the presence of avian influenza virus (AIV), pathogenic properties of AIV subtypes, especially of hemagglutinin (H) subtypes H5 and H7, and a possible association between LBM and non-LBM infections. Ten H subtypes of AIV were isolated from the LBM specimens: H1, H2, H3, H4, H5, H6, H7, H9, H10, and H11. During this period, the 10 subtypes also were isolated from birds in non-LBM premises. In the LBMs, subtypes H2, H3, H4, H6, H7, and H11 were present for 5-8 yr despite efforts to clean and disinfect the premises. The H5 or H7 subtypes present during the same year in both LBMs and non-LBMs within a state or in contiguous states were (subtype/year): H5N2/1993, 1999, and H7N2/1994-99. The AIV subtypes including the H5 and H7 that were evaluated for pathogenicity in chickens were low pathogenic. The deduced amino acid sequence at the H cleavage site of H5 and H7 subtypes was consistent with those of low pathogenic AIV. Although the H5N2 and H7N2 subtypes remained low pathogenic, they did undergo mutations and acquired an additional basic amino acid at the H cleavage site; however, the minimum number of basic amino acids in correct sequence (B-X-B-R, where B = basic amino acid, X = need not be basic amino acid, and R = arginine) required for high pathogenicity was lacking. A low pathogenic H5 or H7 subtype may become highly pathogenic by acquiring additional basic amino acids at the H cleavage site. The LBMs have been and will likely continue to be a source of AIV for commercial poultry.

Amino Acid Sequence↗
PubMed1987

[Pro-opiomelanocortin neuronal systems].

Proopiomelanocortin (POMC) is a glycoprotein which serves as a multihormonal precursor for corticotropin (ACTH), lipotropins (beta and gamma-LPH), melanotropins (alpha, beta- and gamma-MSH) and endorphins (alpha-, beta- and gamma-endorphins). This precursor protein is primarily synthesized in corticotrophs of the anterior lobe and in melanotrophs of the intermediate lobe of the pituitary, as well as in other organs or tissues such as the genitourinary tract, the gastrointestinal tract and leukocytes. POMC is also present in the central nervous system (CNS) and numerous studies have been conducted to determine the localization, biosynthesis and functions of POMC-derived peptides. The identification of POMC-neuronal systems has been achieved by combining immuno histochemical studies, biochemical analysis, bioassays and radioimmunoassays. Three groups of perikarya containing various POMC-related peptides have been identified. One of these is located in the arcuate nucleus in the basal hypothalamus and projects towards the septum, thalamus and telencephalon. Some fibers originating from the arcuate nucleus terminate in the nucleus of the solitary tract in the brainstem where a second group of POMC-containing nerve cells are located. The latter innervates both the mesencephalon, the brainstem and the spinal cord. A third group of neurons, which contain alpha-MSH but not other POMC-derivates, has been identified in the zona incerta in the dorso-lateral hypothalamus. Processing of POMC in the cell bodies of the arcuate nucleus follows a similar pattern as in the pituitary intermediate lobe. Endopeptidases called "acid-thiol-arginyl-proteases" cleave the prohormone at paired basic amino acids. The basic residues remaining on the resulting peptides are subsequently eliminated by the joint action of the less specific B-type carboxypeptidases and B-type aminopeptidases. alpha-MSH and beta-endorphin are among the major end products. Enzymatic modifications including N-alpha-acetylation by opiomelanotropin-acetyltransferase (OMAT) and/or C-terminal amidation by peptidyl-glycine alpha-amidating monooxygenase (PAM) occur after proteolytic processing. However, the rate of acetylation observed in hypothalamic POMC neurons is much lower than in the melanotrophs of the pars intermedia. Acetylation of MSH and endorphin is crucial in determining the biological potency of these peptides. Desacetyl alpha-MSH is far less active than alpha-MSH (monoacetyl alpha-MSH), whereas acetylated beta-endorphin has no opiate activity. The mechanisms regulating the activity of POMC-containing neurons are still unknown.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1993

Structure and function of eukaryotic proprotein processing enzymes of the subtilisin family of serine proteases.

Production of a broad spectrum of regulatory proteins in eukaryotes occurs via an intricate cascade of biosynthetic and secretory processes. Often these proteins initially are synthesized as parts of higher molecular weight, but inactive, precursor proteins. Specific endoproteolytic processing of these proproteins is required to generate the regulatory proteins in a mature and biologically active form. Such endoproteolysis generally occurs at cleavage sites consisting of particular sequence motifs of basic amino acids, often paired basic residues. This phenomenon, first observed almost 25 years ago, has intrigued scientists ever since then. Nevertheless, the responsible enzymes remained elusive for long. The first known eukaryotic enzyme with the exquisite cleavage specificity for paired basic amino acid residues was the prohormone processing enzyme kexin (EC 3.4.21.61), a subtilisin-like serine protease that is encoded by the KEX2 gene of yeast Saccharomyces cerevisiae. Recently, a number of kexin-like mammalian proprotein-processing enzymes were discovered. The enzyme furin, which is encoded by the fur gene, was the first and can be considered the prototype of a mammalian subclass of subtilisin-like serine proteases. It is predicted to contain a "prepro" domain, a subtilisin-like catalytic domain, a middle domain, a cysteine-rich region, a transmembrane anchor, and a cytoplasmic domain. Furin is expressed in a wide variety of tissues, perhaps even in all tissues. In all likelihood, it is the enzyme responsible for the proteolytic bioactivation of a wide variety of precursor proteins. Two other novel mammalian proprotein-processing enzymes are PC1 (also known as PC3) and PC2. Some of the protein domains of these enzymes resemble those in kexin and furin, however, there are also differences. The PC1/PC3 and PC2 enzymes exhibit a more restricted expression pattern than furin. It has been suggested that PC1/PC3 and PC2 are involved primarily in the processing of prohormones within the regulated secretory pathway of cells of endocrine and neural tissue. Recently, the coding sequences for two other candidate mammalian proprotein-processing enzymes were identified. They were called PACE4 and PC4. Like that of furin, the tissue distribution of PACE4 is widespread. PC4, however, may represent a candidate for a precursor-processing endoprotease that is specifically expressed in the testicular germ cells. Finally, DNA sequences encoding kexin- and furin-like candidate pro-protein-processing enzymes have been identified in Drosophila melanogaster, Dfur1 and Dfur2 genes; in Xenopus laevis, Xen-14 gene; and in Caenorhabditis elegans, bli-4 gene.(ABSTRACT TRUNCATED AT 400 WORDS)

Amino Acid Sequence↗
PubMed1994

ATP- and antizyme-dependent endoproteolysis of ornithine decarboxylase to oligopeptides by the 26 S proteasome.

Previously we reported that ornithine decarboxylase (ODC) is degraded ATP-dependently by the 26 S proteasome in the presence of antizyme (AZ), an ODC inhibitor (Murakami, Y., Matsufuji, S., Kameji, T., Hayashi, S., Igarashi, K., Tamura, T., Tanaka, K., and Ichihara, A. (1992) Nature 360, 597-599). Here we examined the cleavage of ODC by the 26 S proteasome. When ODC purified from ODC-overproducing cells was incubated with the 26 S proteasome and with AZ fused with maltose-binding protein (MBP) in the presence of ATP, ODC was degraded specifically without appreciable breakdown of MBP-AZ. The major degradation products of ODC, which were separated by high performance liquid chromatography on a reverse-phase column, were identified by N-terminal amino acid sequencing. The 26 S proteasome generated a variety of short peptides of 5-11 amino acid residues derived from regions throughout the ODC sequence. No detectable amounts of free amino acid residues were produced, indicating endoproteolytic degradation of ODC by the 26 S proteasome. Their major sites for cleavage of ODC by the 26 S proteasome were on the carboxyl sides of neutral/hydrophobic amino acid residues, but a few were on those of acidic or basic amino acid residues. These results demonstrate that the 26 S proteasome causes exhaustive endoproteolysis of the naturally occurring short-lived protein ODC in a multicatalytic and ATP-dependent manner.

Adenosine Triphosphate↗
PubMed1995

Polypeptide amino acid composition and isoelectric point. II. Comparison between experiment and theory.

Experimental isoelectric points and amino acid compositional data for 58 proteins were compiled and organized. The experimental isoelectric points correlated well with the acidic to basic amino acid molar ratio. This agreement proved the usefulness of a recently presented analytical expression correlating explicitly protein isoelectric point to acid-base composition. Regressed acidic and basic dissociation constants were determined to be pK(alpha) = 4.9 and pK(beta) = 10.0, in fair agreement with the expected values of pK(alpha) = 4.2 and pK(beta) = 11.2. Theoretical isoelectric points determined by a more complete computational procedure were on the average in as good an agreement with the experimental values as those calculated via the theoretical approximation using the regressed dissociation constants. Thus, the analytical approximation is a powerful tool for the convenient and accurate calculation of protein isoelectric point from the amino acid composition.

Amino Acids↗
PubMed1975

Tissue specificity of nuclear acidic proteins isolated from bovine brain and adrenal medulla.

Nuclear acidic proteins from bovine brain and adrenal medulla demonstrated dissimilar electophoretic and chemical profiles. The amino acid analysis of the acidic nuclear protein fraction isolated from these tissues revealed some variation in the ratio of acidic to basic amino acids. The estimation of free carboxylic acid groups confirmed the more acidic nature of the brain proteins. In comparing the acrylamide gels either visually or optically, several electrophoretically specific bands were apparent. Although the total number of protein bands from each tissue was approximately the same, the adrenal medulla contained a larger proportion of the more positively charged proteins. These observations are interpreted to indicate that the nuclear acidic protein from brain and adrenal medulla may show functional variation.

Adrenal Medulla↗
PubMed1999

Cloning and characterization of a thermostable cellobiose dehydrogenase from Sporotrichum thermophile.

Cellobiose dehydrogenase (CDH) is an extracellular hemoflavoenzyme produced by several wood-degrading fungi. CDH contains one heme b and one FAD per molecule and oxidizes cellobiose to cellobionolactone in the presence of cytochrome c. In this report, a thermostable CDH from the thermophilic ascomycete Sporotrichum thermophile has been purified, cloned, and characterized. The temperature optimum for this CDH reaction was 60 degrees C, and the activation energy for the reaction was 26.3 kJ/mol. The Km and kcat were temperature-dependent and increased as reaction temperature increased. These kinetic properties prove that this CDH is truly thermophilic. A 2.8-kb cDNA was isolated by screening an expression library of S. thermophile with a polyclonal antisera raised against Phanerochaete chrysosporium CDH. The cDNA encoded an 807-amino-acid protein with a predicted mass of 86,332 Da. S. thermophile CDH is organized into three domains, an N-terminal flavin domain, a middle heme domain, and a C-terminal cellulose-binding domain, which shows sequence similarity with the cellulose-binding domains of endoglucanases and cellobiohydrolases from Trichoderma reesei. Comparison with the CDH sequences of P. chrysosporium and Trametes versicolor identified Met 95 and His 143 as potential heme coordinations. EFIG, LGGPM, and VNSTH motifs in the heme domain and the XRXPXTDXPSXDGXRY motif in the flavin domain were identified as CDH-specific motifs. With regard to the amino acid composition, S. thermophile CDH has more disulfide linkages and acidic and basic amino acids compared to CDHs from P. chrysosporium and T. versicolor.

Amino Acid Sequence↗
PubMed1983

Purification and partial characterization of the myelin-associated glycoprotein from adult rat brain.

The myelin-associated glycoprotein was purified from rat central nervous system myelin by selective extraction with lithium diiodosalicylate-phenol followed by gel filtration on a column of Sepharose CL-6B. Amino acid analysis of the purified glycoprotein revealed an excess of acidic over basic amino acids and a relatively high content of nonpolar residues. On the basis of weight, the molecule is about one-third carbohydrate consisting of 5% fucose, 23% mannose, 20% galactose, 34% N-acetylglucosamine, and 18% N-acetylneuraminic acid.

Amino Acids↗
PubMed2002

A novel synthesis of N-methyl asparagine, arginine, histidine, and tryptophan.

[reaction: see text] N-Methyl amino acid residues in peptides modify several pharmacologically useful parameters, but synthesis of alkylated peptides is hampered by unavailability of N-methylated monomers. The syntheses of four N-methyl amino acids with basic side chains are presented. The side chains of these basic amino acids needed to be specially protected or constructed. This completes the set of 20 common L-amino acid N-methyl derivatives prepared via 5-oxazolidinone intermediates by our group.

Arginine↗
PubMed2002

Purification, characterization, and in vitro mineralization studies of a novel goose eggshell matrix protein, ansocalcin.

Biomineralization is an important process in which hard tissues are generated through mineral deposition, often assisted by biomacromolecules. Eggshells, because of their rapid formation via mineralization, are chosen as a model for understanding the fundamentals of biomineralization. This report discusses purification and characterization of various proteins and peptides from goose eggshell matrix. A novel 15-kDa protein (ansocalcin) was extracted from the eggshell matrix, purified, and identified and its role in mineralization evaluated using in vitro crystal growth experiments. The complete amino acid sequence of ansocalcin showed high homology to ovocleidin-17, a chicken eggshell protein, and to C-type lectins from snake venom. The amino acid sequence of ansocalcin was characterized by the presence of acidic and basic amino acid multiplets. In vitro crystallization experiments showed that ansocalcin induced pits on the rhombohedral faces at lower concentrations (<50 microg/ml). At higher concentrations, the nucleation of calcite crystal aggregates was observed. Molecular weight determinations by size exclusion chromatography and sodium dodecyl sulfate -polyacrylamide gel electrophoresis showed reversible concentration-dependent aggregation of ansocalcin in solution. We propose that such aggregated structures may act as a template for the nucleation of calcite crystal aggregates. Similar aggregation of calcite crystals was also observed when crystallizations were performed in the presence of whole goose eggshell extract. These results show that ansocalcin plays a significant role in goose eggshell calcification.

Alkylation↗
PubMed1976

Antigenically active nonhistone chromatin proteins in cancer cells.

Two-dimensional polyacrylamide gel electrophoresis shows that in nuclei of Novikoff hepatoma ascites cells there are approximately 75 proteins in the chromatin fraction soluble in 3 M NaCl:7 M urea. Dialysis of this fraction to an ionic strength of 0.15 produces a soluble fraction and a precipitate. The proteins in the soluble fraction have been reported to be active in gene control. Antibodies to the soluble fraction distribute diffusely throughout the nucleus, and antibodies to the precipitate localized primarily in the nucleolus and the nuclear ribonucleoprotein network. The nucleolar proteins differ from the extranucleolar proteins in antigenicity and labeling patterns. The development of methods for isolation, purification, and identification of nuclear proteins provided the opportunity for analysis of chromatin antigens in tumor cells. Utilizing two-dimensional preparative polyacrylamide gel techniques as well as conventional procedures, several nuclear proteins have been isolated in electrophoretically homogeneous states including protein A-24, a histone-like nonhistone protein; C-14, a protein that stimulates nucleolar RNA polymerase; and a chromatin antigen soluble in 3 M NaCl:7 M urea that remains soluble after dialysis to 0.15 M NaCl to precipitate the histones and the DNA. This antigen has been found in the chromatin of both the Novikoff hepatoma and the Walker 256 carcinosarcoma but not in the chromatin of either normal or regenerating liver. It is a nonhistone nuclear protein as indicated by its amino acid analysis in which the ratio of the number of acidic to basic amino acids is approximately 1.4. Further studies are in progress on the function and structure of this chromatin protein. As an approach to analysis of relative rates of synthesis of this antigen and otherproteins, the products of translation of messenger RNA of Novikoff hepatoma and normal liver are being analyzed by autoradiography of two-dimensional electrophoretic gels.

Animals↗
PubMed1999

Involvement of Arg-328, Arg-334 and Arg-342 of DnaA protein in the functional interaction with acidic phospholipids.

We reported previously that three basic amino acids (Arg-360, Arg-364 and Lys-372) of DnaA protein are essential for its functional interaction with cardiolipin. In this study, we examined the effect of mutation of some basic amino acids in a potential amphipathic helix (from Lys-327 to Ile-345) of DnaA protein on this interaction. ATP binding to the mutant DnaA protein, in which Arg-328, Arg-334 and Arg-342 were changed to acidic amino acids, was less inhibited by cardiolipin than that of the wild-type protein, as was the case for mutant DnaA protein with mutations of Arg-360, Arg-364 and Lys-372. A mutant DnaA protein with mutations of all six basic amino acids showed the most resistance to the inhibition of ATP binding by cardiolipin. These results suggest that Arg-328, Arg-334 and Arg-342, like Arg-360, Arg-364 and Lys-372, are also involved in the functional interaction between DnaA protein and acidic phospholipids.

Adenosine Diphosphate↗
PubMed1982

Molecular cloning and nucleotide sequence of full-length of cDNA coding for porcine gastrin.

We have cloned in EScherichia coli a cDNA copy of mRNA coding for the porcine antral mucosal hormone preprogastrin. Full-length double-stranded cDNA was synthesized and inserted into the Pst I endonuclease site in plasmid pBR322 by using a homopolymeric extension technique. A partial cDNA clone was used as a probe to identify a complete cDNA clone in a cDNA library by colony hybridization. Four positive clones were isolated, one of which corresponded to porcine preprogastrin mRNA. The nucleotide sequence of the cDNA insert (602 nucleotides) revealed 312 nucleotides in the entire mRNA coding region, 61 nucleotides in the 5' untranslated region, 86 nucleotides in the 3'untranslated region, and a poly(A) tail of 86 nucleotides. Gastrin is located near the carboxyl end of preprogastrin and is flanked at both its amino and carboxyl ends by a pair of basic amino acid residues. The presence of glycine and a pair of basic amino acid residues adjacent in the carboxyl-terminal phenylalanine of gastrin indicates that the glycine and a pair of basic amino acid residues may be required for the enzymatic amidation of phenylalanine to phenylalanine amide.

Animals↗
PubMed2004

The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia.

Familial parkinsonism and dementia with cortical and subcortical Lewy bodies is uncommon, and no genetic defect has been reported in the previously described sibships. We present a Spanish family with autosomal dominant parkinsonism, dementia, and visual hallucinations of variable severity. The postmortem examination showed atrophy of the substantia nigra, lack of Alzheimer pathology, and numerous Lewy bodies which were immunoreactive to alpha-synuclein and ubiquitin in cortical and subcortical areas. Sequencing of the alpha-synuclein gene showed a novel, nonconservative E46K mutation in heterozygosis. The E46K mutation was present in all affected family members and in three young asymptomatic subjects, but it was absent in healthy and pathological controls. The novel mutation, that substitutes a dicarboxylic amino acid, glutamic acid, with a basic amino acid such as lysine in a much conserved area of the protein, is likely to produce severe disturbance of protein function. Our data show that, in addition to the previously described hereditary alpha-synucleinopathies, dementia with Lewy bodies is related to mutation of alpha-synuclein.

Aged↗