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PMID: 8158648 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

pIV, a filamentous phage protein that mediates phage export across the bacterial cell envelope, forms a multimer.

Journal of molecular biology ·Vol. 238 ·No. 2 ·1994-04-29 ·Pages 187-98

Kazmierczak BI, Mielke DL, Russel M, Model P

Abstract

Filamentous phage pIV is an outer membrane protein required for phage assembly and secretion. Chemical cross-linking and sedimentation experiments have been used to demonstrate that pIV from f1-infected Escherichia coli exists as a homo-multimer, probably composed of 10 to 12 subunits. pIV secreted from spheroplasts remains soluble and does not form multimers. Synthesis of pIV from distantly related filamentous phages or from a bacterial homolog that participates in a specialized form of extra-cellular protein secretion in the same cell with pIVf1 resulted in the formation of mixed multimers. This suggests that the homologous proteins themselves form homo-multimers. These structures could form gated channels that conduct assembling phage or specific substrate proteins across the outer membrane to the extracellular milieu.

MeSH Terms
Bacterial Proteins/chemistry,metabolism Biopolymers Centrifugation, Density Gradient Coliphages/chemistry Cross-Linking Reagents Dickeya chrysanthemi/chemistry Escherichia coli/metabolism Inovirus/chemistry Precipitin Tests Spheroplasts/metabolism Viral Proteins/chemistry,metabolism
Chemicals
Bacterial Proteins Biopolymers Cross-Linking Reagents Viral Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Kazmierczak B I
Rockefeller University, New York, NY 10021.
Mielke D L
Russel M
Model P
Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
Published
1994-04-29
Pages
187-98
Language
English
Region
England
NLM ID
2985088R
Subset
IM
Grants
NIAID NIH HHS · AI07233 · United States
NIGMS NIH HHS · GM07739 · United States
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