Gene for staphylococcal protein A.
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Journal: 1983/April - Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
PUBMED: 6338496
Abstract:
The gene for protein A from Staphylococcus aureus was cloned into pBR322 in Escherichia coli. An immunoassay was used to detect production of the protein. Protein A produced in E. coli was found in the periplasmic space and was purified and concentrated by IgG-Sepharose affinity chromatography. DNA sequence assay of the gene revealed a region with the general features of a prokaryotic signal peptide and a fifth structural region homologous to the four repetitive regions found earlier by amino acid sequence determination of the mature protein. Upstream from the structural gene there is a possible promoter region and a ribosomal binding sequence typical of gram-positive bacteria. The initiation codon is TTG.
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Proc Natl Acad Sci U S A 80(3): 697-701
PMID: 6338496

Gene for staphylococcal protein A.

Abstract

The gene for protein A from Staphylococcus aureus was cloned into pBR322 in Escherichia coli. An immunoassay was used to detect production of the protein. Protein A produced in E. coli was found in the periplasmic space and was purified and concentrated by IgG-Sepharose affinity chromatography. DNA sequence assay of the gene revealed a region with the general features of a prokaryotic signal peptide and a fifth structural region homologous to the four repetitive regions found earlier by amino acid sequence determination of the mature protein. Upstream from the structural gene there is a possible promoter region and a ribosomal binding sequence typical of gram-positive bacteria. The initiation codon is TTG.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Björk I, Petersson BA, Sjöquist J. Some physiochemical properties of protein A from Staphylococcus aureus. Eur J Biochem. 1972 Sep 25;29(3):579–584. [PubMed] [Google Scholar]
  • Forsgren A, Sjöquist J. "Protein A" from S. aureus. I. Pseudo-immune reaction with human gamma-globulin. J Immunol. 1966 Dec;97(6):822–827. [PubMed] [Google Scholar]
  • Goding JW. Use of staphylococcal protein A as an immunological reagent. J Immunol Methods. 1978;20:241–253. [PubMed] [Google Scholar]
  • Movitz J. A study on the biosynthesis of protein A in Staphylococcus aureus. Eur J Biochem. 1974 Oct 1;48(1):131–136. [PubMed] [Google Scholar]
  • Movitz J. Formation of extracellular protein A by Staphylococcus aureus. Eur J Biochem. 1976 Sep;68(1):291–299. [PubMed] [Google Scholar]
  • Winblad S, Ericson C. Sensitized sheep red cells as a reactant for Staphylococcus aureus protein A. Methodology and epidemiology with special reference to weakly reacting methicillin-resistant strains. Acta Pathol Microbiol Scand B Microbiol Immunol. 1973 Feb;81(1):150–156. [PubMed] [Google Scholar]
  • Murray NE, Batten PL, Murray K. Restriction of bacteriophage lambda by Escherichia coli K. J Mol Biol. 1973 Dec 15;81(3):395–407. [PubMed] [Google Scholar]
  • Marinus MG. Location of DNA methylation genes on the Escherichia coli K-12 genetic map. Mol Gen Genet. 1973 Dec 14;127(1):47–55. [PubMed] [Google Scholar]
  • Boyer HW, Roulland-Dussoix D. A complementation analysis of the restriction and modification of DNA in Escherichia coli. J Mol Biol. 1969 May 14;41(3):459–472. [PubMed] [Google Scholar]
  • Bolivar F, Rodriguez RL, Greene PJ, Betlach MC, Heyneker HL, Boyer HW, Crosa JH, Falkow S. Construction and characterization of new cloning vehicles. II. A multipurpose cloning system. Gene. 1977;2(2):95–113. [PubMed] [Google Scholar]
  • Soberon X, Covarrubias L, Bolivar F. Construction and characterization of new cloning vehicles. IV. Deletion derivatives of pBR322 and pBR325. Gene. 1980 May;9(3-4):287–305. [PubMed] [Google Scholar]
  • Roberts TM, Swanberg SL, Poteete A, Riedel G, Backman K. A plasmid cloning vehicle allowing a positive selection for inserted fragments. Gene. 1980 Dec;12(1-2):123–127. [PubMed] [Google Scholar]
  • Michel B, Palla E, Niaudet B, Ehrlich SD. DNA cloning in Bacillus subtilis. III. Efficiency of random-segment cloning and insertional inactivation vectors. Gene. 1980 Dec;12(1-2):147–154. [PubMed] [Google Scholar]
  • Sjöström JE, Löfdahl S, Philipson L. Transformation reveals a chromosomal locus of the gene(s) for methicillin resistance in Staphylococcus aureus. J Bacteriol. 1975 Sep;123(3):905–915.[PMC free article] [PubMed] [Google Scholar]
  • Tanaka T, Weisblum B. Construction of a colicin E1-R factor composite plasmid in vitro: means for amplification of deoxyribonucleic acid. J Bacteriol. 1975 Jan;121(1):354–362.[PMC free article] [PubMed] [Google Scholar]
  • Birnboim HC, Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979 Nov 24;7(6):1513–1523.[PMC free article] [PubMed] [Google Scholar]
  • Morrison DA. Transformation and preservation of competent bacterial cells by freezing. Methods Enzymol. 1979;68:326–331. [PubMed] [Google Scholar]
  • Maxam AM, Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. [PubMed] [Google Scholar]
  • Persson H, Signäs C, Philipson L. Purification and characterization of an early glycoprotein from adenovirus type 2-infected cells. J Virol. 1979 Mar;29(3):938–948.[PMC free article] [PubMed] [Google Scholar]
  • Jelenc PC. Rapid purification of highly active ribosomes from Escherichia coli. Anal Biochem. 1980 Jul 1;105(2):369–374. [PubMed] [Google Scholar]
  • Heppel LA. Selective release of enzymes from bacteria. Science. 1967 Jun 16;156(3781):1451–1455. [PubMed] [Google Scholar]
  • HEPPEL LA, HARKNESS DR, HILMOE RJ. A study of the substrate specificity and other properties of the alkaline phosphatase of Escherichia coli. J Biol Chem. 1962 Mar;237:841–846. [PubMed] [Google Scholar]
  • Wagner EG, Jelenc PC, Ehrenberg M, Kurland CG. Rate of elongation of polyphenylalanine in vitro. Eur J Biochem. 1982 Feb;122(1):193–197. [PubMed] [Google Scholar]
  • Hjelm H, Hjelm K, Sjöquist J. Protein A from Staphylococcus aureus. Its isolation by affinity chromatography and its use as an immunosorbent for isolation of immunoglobulins. FEBS Lett. 1972 Nov 15;28(1):73–76. [PubMed] [Google Scholar]
  • Inouye M, Halegoua S. Secretion and membrane localization of proteins in Escherichia coli. CRC Crit Rev Biochem. 1980;7(4):339–371. [PubMed] [Google Scholar]
  • McLaughlin JR, Murray CL, Rabinowitz JC. Unique features in the ribosome binding site sequence of the gram-positive Staphylococcus aureus beta-lactamase gene. J Biol Chem. 1981 Nov 10;256(21):11283–11291. [PubMed] [Google Scholar]
  • Shine J, Dalgarno L. Determinant of cistron specificity in bacterial ribosomes. Nature. 1975 Mar 6;254(5495):34–38. [PubMed] [Google Scholar]
  • Neu HC, Heppel LA. The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J Biol Chem. 1965 Sep;240(9):3685–3692. [PubMed] [Google Scholar]
  • Forsgren A. Pathogenicity of Staphylococcus aureus mutants in general and local infections. Acta Pathol Microbiol Scand B Microbiol Immunol. 1972;80(4):564–570. [PubMed] [Google Scholar]
  • Mudd S. Resistance against Staphylococcus aureus. JAMA. 1971 Dec 13;218(11):1671–1673. [PubMed] [Google Scholar]
  • Bansal SC, Bansal BR, Thomas HL, Siegel PD, Rhoads JE, Jr, Cooper DR, Terman DS, Mark R. Ex vivo removal of serum IgG in a patient with colon carcinoma: some biochemical, immunological and histological observations. Cancer. 1978 Jul;42(1):1–18. [PubMed] [Google Scholar]
  • Lindmark R, Movitz J, Sjöquist J. Extracellular protein A from a methicillin-resistant strain of Staphylococcus aureus. Eur J Biochem. 1977 Apr 15;74(3):623–628. [PubMed] [Google Scholar]
  • Kroyer J, Chang S. The promoter-proximal region of the Bacillus licheniformis penicillinase gene: Nucleotide sequence and predicted leader peptide sequence. Gene. 1981 Dec;15(4):343–347. [PubMed] [Google Scholar]
  • Palva I, Pettersson RF, Kalkkinen N, Lehtovaara P, Sarvas M, Söderlund H, Takkinen K, Käriäinen L. Nucleotide sequence of the promoter and NH2-terminal signal peptide region of the alpha-amylase gene from Bacillus amyloliquefaciens. Gene. 1981 Oct;15(1):43–51. [PubMed] [Google Scholar]
  • Rosenberg M, Court D. Regulatory sequences involved in the promotion and termination of RNA transcription. Annu Rev Genet. 1979;13:319–353. [PubMed] [Google Scholar]
Copyright notice
Abstract
The gene for protein A from Staphylococcus aureus was cloned into pBR322 in Escherichia coli. An immunoassay was used to detect production of the protein. Protein A produced in E. coli was found in the periplasmic space and was purified and concentrated by IgG-Sepharose affinity chromatography. DNA sequence assay of the gene revealed a region with the general features of a prokaryotic signal peptide and a fifth structural region homologous to the four repetitive regions found earlier by amino acid sequence determination of the mature protein. Upstream from the structural gene there is a possible promoter region and a ribosomal binding sequence typical of gram-positive bacteria. The initiation codon is TTG.
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