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Showing papers on "Peptide sequence published in 1980"


Journal ArticleDOI
TL;DR: In this article, it was shown that the β-lactamases have a polyphyletic origin and all the enzymes of currently known amino acid sequence belong to one homology group, called class A enzymes.
Abstract: The beta-lactamases are widely distributed in both Gram-positive and Gram-negative bacteria. They all inactivate penicillins and cephalosporins by opening the beta-lactam ring. Many varieties of the enzyme can be distinguished on the basis of their catalytic and molecular properties, but only amino acid sequence determination gives information upon which a molecular phylogeny can be based. The present evidence suggests that the beta-lactamases have a polyphyletic origin. All the beta-lactamases of currently known amino acid sequence belong to one homology group, here called class A enzymes. Class B consists of the mechanistically distinct Bacillus cereus beta-lactamase II, which preliminary partial sequence analysis suggests to be structurally unrelated to the class A enzymes. It is predicted that sequence analysis will show that further classes will need to be created to account for particular beta-lactamases of distinctive molecular and mechanistic properties.

1,624 citations



Journal ArticleDOI
TL;DR: Results suggest that selective binding of the COOH-terminal dipeptide residue is an impor tan t dete rminant of both the substrate specificity of angiotensin-converting enzyme and the degree of rate stimulation by chloride ion, and that the nature of this selective binding can be further clarified by studying competitive inhibition of dpeptides of vary ing structure.

721 citations


Journal ArticleDOI
05 Jun 1980-Nature
TL;DR: A chemical detection system based on fragmentation of peptides in tissue extracts followed by identification of certain of these peptide fragments having distinct chemical features is proposed and several previously unknown peptide amides in porcine upper small intestinal tissues are found.
Abstract: Naturally occurring peptides with biological actions have in most cases been detected by observing their biological activities in crude extracts and their isolation has been followed using bioassays. As a complement to the classical biological detection systems, we have proposed a chemical detection system based on fragmentation of peptides in tissue extracts followed by identification of certain of these peptide fragments having distinct chemical features. One such chemical feature is the C-terminal amide structure which is characteristic of many biologically active peptides. We have devised a chemical assay method for peptides having such a structure and have found several previously unknown peptide amides in procine upper small intestinal tissues. We report here the isolation and characterization of two of them, designated PHI and PYY. PHI is related to secretin, vasoactive intestinal polypeptide (VIP, glucagon and gastric inhibitory polypeptide (GIP); PYY is related to the pancreatic polypeptide and to neurotensin. Both peptides exhibit biological activities and appear to be present not only in the intestine but also in brain.

667 citations



Journal ArticleDOI
01 Jun 1980-Cell
TL;DR: It is demonstrated that mum and mus heavy chains are encoded by separate mRNAs of 2.7 and 2.4 kb, respectively, and it is proposed that comparable C terminal segments also will be found in other membrane-bound immunoglobulin heavy chains.

588 citations


Journal ArticleDOI
TL;DR: Comparison with the nearly complete sequences of the bovine uterus and rat testis modulator proteins reported by other laboratories indicates that this ubiquitous calcium-dependent regulatory protein does not occur in tissue-specific forms, commensurate with the proposed function of modulator protein as a mediator of calcium-second messenger function in eukaryotic cells.

554 citations


Journal ArticleDOI
27 Jun 1980-Science
TL;DR: Genealogical analysis suggests that divergence from a common ancestral gene occurred early in the evolution of the receptor, and argues that each of the four subunits plays a functional role in the receptor's physiological action.
Abstract: The acetylcholine receptor from the electric ray Torpedo californica is composed of five subunits; two are identical and the other three are structurally related to them. Microsequence analysis of the four polypeptides demonstrates amino acid homology among the subunits. Further sequence analysis of both membrane-bound and Triton-solubilized, chromatographically purified receptor gave the stoichiometry of the four subunits (40,000:50,000:60,000:65,000 daltons) as 2:1:1:1, indicating that this protein is a pentameric complex with a molecular weight of 255,000 daltons. Genealogical analysis suggests that divergence from a common ancestral gene occurred early in the evolution of the receptor. This shared ancestry argues that each of the four subunits plays a functional role in the receptor's physiological action.

554 citations


Journal ArticleDOI
02 Oct 1980-Nature
TL;DR: A human leukocyte interferon cDNA was enzymatically synthesized, inserted into the vector pBR322, and cloned in Escherichia coli, and protected squirrel monkeys from lethal encephalomyocarditis virus infection.
Abstract: A human leukocyte interferon cDNA was enzymatically synthesized, inserted into the vector pBR322, and cloned in Escherichia coli. The DNA sequence codes for a 23-amino acid signal peptide followed by an interferon polypeptide of 165 amino acids. An expression plasmid was constructed which permits the synthesis in E. coli of 2.5 x 10(8) units of interferon per litre of culture. This LeIF protected squirrel monkeys from lethal encephalomyocarditis virus infection.

511 citations


Journal ArticleDOI
TL;DR: In this paper, the authors used cloned actin sequences from Dictyostelium discoideum to identify and clone the actin gene in yeast and determined the nucleotide sequence of that gene and its flanking regions.
Abstract: The yeast Saccharomyces cerevisiae is known to contain the highly conserved and unbiquitous protein actin. We have used cloned actin sequences from Dictyostelium discoideum to identify and clone the actin gene in yeast. Hybridization to genomic fragments of yeast DNA suggest that there is a single actin gene in yeast. We have determined the nucleotide sequence of that gene and its flanking regions. The sequence of the gene reveals an intervening sequence of 309 base pairs in the coding sequences at the 5' end of the gene. The existence and location of the intervening sequence was verified by using the dideoxy chain termination technique to determine the sequence at the 5' terminus of the actin mRNA. The similarity of the splice junction sequences in this gene to those found in higher eukaryotes suggests that yeast must possess a similar splicing enzyme.

463 citations


Journal ArticleDOI
01 May 1980-Cell
TL;DR: Analysis of the cloned DNA confirms the linkage arrangement of the two adult α-globin genes (α1 and α2) previously derived from genomic blotting experiments and identifies two additional closely linked α-like genes.

Journal ArticleDOI
01 Oct 1980-Cell
TL;DR: The complete nucleotide sequence of the human β-globin gene is reported to provide the basis for comparing normal β- globin genes with those obtained from the DNA of individuals with genetic defects in hemoglobin expression.

Journal ArticleDOI
20 Nov 1980-Nature
TL;DR: The genes coding for the three membrane polypeptides of Semliki Forest virus have been sequenced and the primary structures of the proteins deduced and the amino acid sequence gives further insight into how the transmembrane structure of the three-chain virus membrane glycoprotein is generated in the infected cell.
Abstract: The genes coding for the three membrane polypeptides of Semliki Forest virus have been sequenced and the primary structures of the proteins deduced. The amino acid sequence gives further insight into how the transmembrane structure of the three-chain virus membrane glycoprotein is generated in the infected cell.

Journal ArticleDOI
TL;DR: Urotensin II, a peptide hormone from the caudal neurosecretory system of the teleost, Gillichthys mirabilis, was isolated by using classical chromatographic techniques and high-performance liquid chromatography (HPLC) to establish its structure.
Abstract: Urotensin II, a peptide hormone from the caudal neurosecretory system of the teleost, Gillichthys mirabilis, was isolated by using classical chromatographic techniques and high-performance liquid chromatography (HPLC). Direct microtechniques for sequence determination were used to establish its structure. Urotensin II from Gillichthys is a 1363-dalton dodecapeptide with the amino acid sequence Ala-Gly-Thr-Ala-Asp-Cys-Phe-Trp-Lys-Tyr-Cys-Val. This sequence is homologous with somatostatin in positions 1 and 2 and 7-9. The sequence has been verified by the production of a bioactive synthetic urotensin II. The possible chemical and physiological significance of its homology to somatostatin is discussed.

Journal ArticleDOI
01 Aug 1980-Virology
TL;DR: The results suggest that the oligopeptides competitively interfere with the N-terminal region of the F 1 or HA 2 polypeptides of paramyxoviruses or myxoviruse, respectively, providing a possible new approach to chemical inhibition of viral replication.

Journal ArticleDOI
TL;DR: The complete nucleotide sequence of the actin gene from Saccharomyces cerevisiae has been determined and its primary structure, especially the NH2-terminal third of the protein, is highly conserved during evolution.
Abstract: The complete nucleotide sequence of the actin gene from Saccharomyces cerevisiae has been determined. The coding region is interrupted by a 304-base-pair intervening sequence that is located within the triplet coding for amino acid 4. DNA sequences of the intron-exon junctions are similar to those found in higher eukaryotes and can be aligned such that the intron starts with the dinucleotide 5'-G-T-3' and ends with 5'-A-G-3'. Regions fo homology within the sequences upstream from the initiation codon and those following the termination codon have been detected between the yeast iso-1-cytochrome c gene and the actin gene. As deduced from the nucleotide sequence, yeast actin has 374 amino acid residues. Its primary structure, especially the NH2-terminal third of the protein, is highly conserved during evolution.

Journal ArticleDOI
01 Jul 1980-Cell
TL;DR: Results show that the carboxy-terminal amino acid sequence of beta-lactamase is essential to successful transport across the cytoplasmic membrane, and suggest that the presence (and probably also the act of removal) of the signal sequence does not suffice to ensure secretion.

Journal ArticleDOI
01 Sep 1980-Cell
TL;DR: The complete sequence of cloned full-length DNA (NS DNA) derived from influenza virus gene 8, which codes for two unique polypeptides, NS1 and NS2, and the sequence of the NS2 mRNA is obtained, indicating that NS1and NS2 overlap by 70 amino acids that are translated from different reading frames.

Journal ArticleDOI
25 Sep 1980-Nature
TL;DR: Comparison of the amino acid sequences of these haemagglutinins with those of other H3 and avian strains reveals theent of sequence changes in antigenic shifts and drifts.
Abstract: Double-stranded DNA copies of the RNA gene coding for the haemagglutinin glycoproteins from human H2 and H3 pandemic strains of influenza virus have been cloned. DNA sequence analysis provides the first reported complete nucleotide sequence of an H2 haemagglutinin gene and a partial sequence (45%) of the H3 gene. The H2 haemagglutinin gene consists of 1,773 nucleotides containing an uninterrupted coding sequence of 1,686 nucleotides specifying a protein of 562 amino acids. Comparison of the amino acid sequences of these haemagglutinins with those of other H3 and avian strains reveals the extent of sequence changes in antigenic shifts and drifts.

Journal ArticleDOI
TL;DR: Plasmid pLC1437a contains DNA from Escherichia coli K12 including fol, the structural gene for dihydrofolate reductase, and the nucleotide sequence for the entire fol gene and its flanking regions from this strain was determined.
Abstract: Plasmid pLC1437a contains DNA from Escherichia coli K12 including fol, the structural gene for dihydrofolate reductase. The fol gene was mapped on this plasmid relative to several restriction endonuclease cleavage sites. fol was also cloned from strain RSO and the nucleotide sequence for the entire fol gene and its flanking regions from this strain was determined. The amino acid sequence predicted from the nucleotide sequence differs in only a few respects from the reported amino acid sequence of dihydrofolate reductase from E. coli B. The major RNA transcripts initiated at the fol promotor in vivo are approximately 550 and 590 nucleotides long. In addition to these, several longer transcripts (up to 1400 nucleotides) are present in lesser amounts. A new procedure is described for 3' end labeling of DNA fragments having blunt ends using E. coli exonuclease III and avian myeloblastoma virus reverse transcriptase.

Journal ArticleDOI
19 Jun 1980-Nature
TL;DR: From the nucleotide sequence of the gene, the complete amino acid sequence of human fibroblast interferon was deduced and the protein is 166 amino acids long and is preceded by a 21-amino acid signal sequence.
Abstract: Chimaeric plasmids containing double-stranded cDNA copies of mRNA induced in human fibroblasts by poly I · C were screened by an RNA selection method. A series of clones to which human fibroblast interferon mRNA selectively hybridized was identified. From the nucleotide sequence of the gene, the complete amino acid sequence of human fibroblast interferon was deduced. The protein is 166 amino acids long and is preceded by a 21-amino acid signal sequence.

Journal ArticleDOI
14 Aug 1980-Nature
TL;DR: Analysis of the βHCG cDNA nucleotide sequence suggests that this extension may have arisen by the loss of the termination codon of an ancestral β-like gene so that most of what was previously the 3′-untranslated region now codes for protein.
Abstract: A 579-base pair approximately full-length cDNA which codes for the 145-amino acid long beta-subunit of human chorionic gonadotropin (HCG) has been cloned in the plasmid vector pBR322 and its complete nucleotide sequence determined. A hydrophobic presequence of 20 amino acids can be identified from the nucleotide sequence. The amino acid sequence of the beta-subunit is known to be related to those of the beta-subunits of the other glycoprotein hormones LH, FSH and TSH, but the beta-subunit of HCG is unique in that it contains a C-terminal extension of about 30 amino acids which has no homologous counterpart in the other three hormones. Analysis of the beta HCG cDNA nucleotide sequence suggests that this extension may have arisen by the loss of the termination codon of an ancestral beta-like gene so that most of what was previously the 3'-untranslated region now codes for protein. The beta-subunit of HCG terminates with the codon UAA located 16 bases before the poly(A) in the sequence AAUAAA. This sequence is believed to be a recognition signal involved in either polyadenylation or processing and therefore has a dual role in this gene, serving both a coding and a regulatory function.

Journal ArticleDOI
TL;DR: The nucleotide sequence of the recA gene of Escherichia coli is determined; this permits the formulation of the primary structure for theRecA protein, which is consistent with the amino acid composition of the tryptic peptides obtained from the RecA protein.
Abstract: We have determined the nucleotide sequence of the recA gene of Escherichia coli; this permits the formulation of the primary structure for the recA protein. This structure is consistent with the amino acid composition of the tryptic peptides obtained from the recA protein. The coding region of the recA gene has 1059 base pairs, which specify 352 amino acids. The recA protein has alanine and phenylalanine as its NH2- and COOH-terminal amino acids, respectively, and has the following amino acid composition: Cys3 Asp20 Asn15 Met9 Thr17 Ser20 Glu30 Gln13 Pro10 Gly35 Ala38 Val22 Ile27 Leu31 Tyr7 Phe10 His2Lys27 Trp2 Arg14. Of the three cysteine residues, only two can be alkylated under reducing and denaturing conditions. The molecular weight of the recA polypeptide is 37,842.

Journal ArticleDOI
31 Jan 1980-Nature
TL;DR: The work leading to the current models of protein secretion is reviewed and the value of bacterial systems in the study of protein transfer across membranes is stressed.
Abstract: Many secreted proteins are synthesised as a large precursor with an additional hydrophobic N-terminal signal sequence that is cleaved by a membrane-bound enzyme. The proteins are secreted as nascent chains. The work leading to the current models of protein secretion is reviewed and the value of bacterial systems in the study of protein transfer across membranes is stressed.

Journal ArticleDOI
TL;DR: The identification of glutamic acid at position 17 represents the first instance where a partially gamma-carboxylated glutamate has been found in a sequence position which is to the NH2-terminal side of a gamma- carboxyglutamate residue.

Journal ArticleDOI
TL;DR: It is determined that the ST toxin with activity assayable in suckling mice (ST I) is genetically distinct from the St toxin assayability in ligated ileal loops (ST II) and that ST I can be responsible for diarrheal disease in different animals.
Abstract: the Escherichia coli heat-stable toxin (ST I) is encoded within a transposon (Tn1681) flanked by inverted repeats of insertion sequence 1 (IS1) [So, M., Heffron, F. & McCarthy, B. J. (1979) Nature (London) 277, 453-456]. By subcloning restriction fragments and by insertion mutagenesis, we located precisely the gene for ST I within the transposon. We determined the complete nucleotide sequence of the central portion of Tn1681 (i.e., that part flanked by IS1) and identified the coding sequence of the toxin. From the nucleotide sequence, we deduced a probable amino acid sequence for ST I. The NH2-terminal portion of the amino acid sequence is extremely hydrophobic and bears a striking resemblance to the signal sequence of the fd phage minor coat protein. By using a subcloned restriction fragment containing the gene for ST I but no IS1 sequences, we determined (i) that the ST toxin with activity assayable in suckling mice (ST I) is genetically distinct from the St toxin assayable in ligated ileal loops (ST II) and (ii) that ST I can be responsible for diarrheal disease in different animals.


Journal ArticleDOI
TL;DR: Antibodies specific for the amino- and carboxy-terminal portions of simian virus 40 large tumor (T) antigen were obtained by immunization of rabbits with synthetic peptides corresponding to these regions by using procedures of general importance for identification and characterization of gene product.
Abstract: Antibodies specific for the amino- and carboxy-terminal portions of simian virus 40 large tumor (T) antigen were obtained by immunization of rabbits with synthetic peptides corresponding to these regions. The amino-terminal synthetic peptide has the sequence Ac-Met-Asp-Lys-Val-Leu-Asn-Arg-(Tyr). The tyrosine residue was introduced in order to couple the peptide to bovine serum albumin with bis-diazotized benzidine. The carboxy-terminal peptide has the sequence Lys-Pro-Pro-Thr-Pro-Pro-Pro-Glu-Pro-Glu-Thr. It was coupled to bovine serum albumin with glutaraldehyde. The antisera against both peptides reacted with large T antigen. The specificity of the immune reaction was demonstrated by inhibition experiments using excess synthetic peptides. Furthermore, fragments of T antigen encoded by the nondefective adenovirus 2-simian virus 40 hybrid viruses Ad2+ND2 and Ad2+ND4, which contain the carboxy terminus and lack the amino terminus of large T antigen, were precipitated only with antiserum to the carboxy-terminal peptide. Small T antigen was not precipitated with either serum, suggesting that the amino terminus of small T antigen has a conformation different from that of large T antigen or that it is sterically hindered by a host protein. The procedures used here are of general importance for identification and characterization of gene product.

Journal ArticleDOI
03 Jan 1980-Nature
TL;DR: The complete variable region sequences from ten antibodies and two myeloma proteins binding α-1,3 dextran suggest that the variable regions of heavy chains are encoded by separate variable (V) and joining (J) gene segments.
Abstract: The complete variable region sequences from ten antibodies and two myeloma proteins binding α-1,3 dextran have been determined. The diversity patterns of these homogeneous antibody molecules suggest that the variable regions of heavy chains are encoded by separate variable (V) and joining (J) gene segments. The most striking feature of these data is the extensive sequence variability of a region that we denote the D (diversity) segment which is located at the junction between the V and J segments in the centre of the third hypervariable region. The D segment diversity may arise from a novel somatic mutational mechanism or may be encoded by multiple D gene segments. For the first time, the amino acid sequence correlates of several V region idiotypes are determined.

Journal ArticleDOI
TL;DR: The amplification in bacteria and the sequence analysis of DNA complementary to rat Prl mRNA support the hypothesis that the Prl and GH genes derive from a common precursor at around 380 million years ago.