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PMID: 1066681 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Structural (shape-maintaining) role of the cell surface glycoprotein of Halobacterium salinarium.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 73 ·No. 8 ·1976-08-00 ·Pages 2687-91

Mescher MF, Strominger JL

Abstract

The obligate halophile, Halobacterium salinarium, maintains a rod-shaped morphology under normal growth conditions. Lactoperoxidase(EC 1.11.1.7;donor:hydrogen-peroxide oxidoreductase)-catalyzed iodination and treatment with proteolytic enzymes were used to demonstrate that the recently described envelope glycoprotein (Mescher, M.F. & Strominger, J.L. (1976) J. Biol. Chem. 251, 2005-2014) is the only major cell surface component of this organism. The morphological changes that accompany alteration of the structure of the glycoprotein by growth in the presence of bacitracin or its removal with proteolytic enzymes strongly suggest that it forms a rigid matrix at the cell surface and is responsible for maintenance of the characteristic rod shape.

MeSH Terms
Bacitracin/pharmacology Bacterial Proteins/physiology Cell Membrane/ultrastructure Glycoproteins/physiology Halobacterium/drug effects,ultrastructure Lactoperoxidase Peptide Hydrolases
Chemicals
Bacterial Proteins Glycoproteins Bacitracin Lactoperoxidase Peptide Hydrolases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Mescher M F
Strominger J L
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22 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.73.8.2687
Published
1976-08-00
Pages
2687-91
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC430713
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.73.8.2687 PMC Full Text View journal details
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