Home LiteratureArticle Details
PMID: 6406428 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Localization and quantitation of proteins characteristic of the complexed membrane of Bacillus subtilis.

Journal of bacteriology ·Vol. 154 ·No. 3 ·1983-06-00 ·Pages 1215-21

Horiuchi S, Marty-Mazars D, Tai PC, Davis BD

Abstract

We prepared antibodies to four proteins (molecular weights, 68,000, 64,000, 45,000, and 31,000) that are characteristic of the complexed (ribosome-bearing) fraction of the membrane of Bacillus subtilis and found that these proteins are immunologically distinct. Quantitation by immunoprecipitation confirmed that the ribosome-free membrane fraction contains much lower concentrations of these four proteins than the complexed-membrane fraction. The 64-kilodalton protein appeared to be attached more loosely than the other proteins, since it was more readily extracted from the membrane. In addition, this protein was also present in the cytosol in an even greater amount than in the membrane. The 68-, 64-, and 31-kilodalton proteins are present in cells in stoichiometrically equivalent amounts.

MeSH Terms
Antibodies, Bacterial Bacillus subtilis/analysis Bacterial Proteins/analysis,immunology Cytosol/analysis Membrane Proteins/analysis,immunology Molecular Weight Octoxynol Polyethylene Glycols/pharmacology Potassium Chloride/pharmacology Precipitin Tests Ribosomes/analysis
Chemicals
Antibodies, Bacterial Bacterial Proteins Membrane Proteins Polyethylene Glycols Potassium Chloride Octoxynol
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Horiuchi S
Marty-Mazars D
Tai P C
Davis B D
References (10)
10 references, click to expand
  1. Selective solubilization of proteins from red blood cell membranes by protein perturbants.
    J Supramol Struct. 1973;1(3):220-32 PMID: 4804837
  2. Radiolabeling of proteins by reductive alkylation with [14C]formaldehyde and sodium cyanoborohydride.
    Anal Biochem. 1978 Jul 1;87(2):562-5 PMID: 567446
  3. Proteins of the outer membrane of gram-negative bacteria.
    Annu Rev Microbiol. 1980;34:369-422 PMID: 6254441
  4. Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum.
    Proc Natl Acad Sci U S A. 1980 Dec;77(12):7112-6 PMID: 6938958
  5. Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein.
    J Cell Biol. 1981 Nov;91(2 Pt 1):551-6 PMID: 7309796
  6. Secretory protein translocation across membranes-the role of the "docking protein'.
    Nature. 1982 Jun 24;297(5868):647-50 PMID: 7088152
  7. Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum.
    Nature. 1982 Oct 21;299(5885):691-8 PMID: 6181418
  8. Regulation of a membrane component required for protein secretion in Escherichia coli.
    Cell. 1982 Aug;30(1):311-9 PMID: 6751561
  9. Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle.
    J Cell Biol. 1982 Nov;95(2 Pt 1):463-9 PMID: 6292235
  10. Proteins of ribosome-bearing and free-membrane domains in Bacillus subtilis.
    J Bacteriol. 1983 Jun;154(3):1381-8 PMID: 6406431
Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1983-06-00
Pages
1215-21
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC217593
Subset
IM
Grants
NIGMS NIH HHS · GM-16835 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]