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PMID: 16547061 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Liberation of zinc-containing L31 (RpmE) from ribosomes by its paralogous gene product, YtiA, in Bacillus subtilis.

Journal of bacteriology ·Vol. 188 ·No. 7 ·2006-04-00 ·Pages 2715-20

Akanuma G, Nanamiya H, Natori Y, Nomura N, Kawamura F

Abstract

We have found that alternative localization of two types of L31 ribosomal protein, RpmE and YtiA, is controlled by the intracellular concentration of zinc in Bacillus subtilis. The detailed mechanisms for the alternation of L31 proteins under zinc-deficient conditions were previously unknown. To obtain further information about this regulatory mechanism, we have studied the stability of RpmE in vivo and the binding affinity of these proteins to ribosomes in vitro, and we have found that liberation of RpmE from ribosomes is triggered by the expression of ytiA, which is induced by the derepression of Zur under zinc-deficient conditions.

MeSH Terms
Bacillus subtilis/metabolism Bacterial Proteins/metabolism Gene Expression Regulation, Bacterial Protein Binding Ribosomes/metabolism Zinc/metabolism
Chemicals
Bacterial Proteins Zinc
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Akanuma Genki
College of Science, Rikkyo University, Toshima-ku Nishi-ikebukuro 3-34-1, Tokyo 171-8501, Japan.
Nanamiya Hideaki
Natori Yousuke
Nomura Naofumi
Kawamura Fujio
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/JB.188.7.2715-2720.2006
Published
2006-04-00
Pages
2715-20
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC1428384
Subset
IM
External Links
PubMed source DOI: 10.1128/JB.188.7.2715-2720.2006 PMC Full Text View journal details
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