Interaction of Streptococcus mutans YidC1 and YidC2 with Translating and Nontranslating Ribosomes

Zht Cheng Wu, Jeanine de Keyzer, Greetje A. Berrelkamp-Lahpor, Arnold J. M. Driessen*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

15 Citations (Scopus)
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Abstract

The YidC/OxaI/Alb3 family of membrane proteins is involved in the biogenesis of integral membrane proteins in bacteria, mitochondria, and chloroplasts. Gram-positive bacteria often contain multiple YidC paralogs that can be subdivided into two major classes, namely, YidC1 and YidC2. The Streptococcus mutans YidC1 and YidC2 proteins possess C-terminal tails that differ in charges (+9 and +14) and lengths (33 and 61 amino acids). The longer YidC2 C terminus bears a resemblance to the C-terminal ribosome-binding domain of the mitochondrial OxaI protein and, in contrast to the shorter YidC1 C terminus, can mediate the interaction with mitochondrial ribosomes. These observations have led to the suggestion that YidC1 and YidC2 differ in their abilities to interact with ribosomes. However, the interaction with bacterial translating ribosomes has never been addressed. Here we demonstrate that Escherichia coli ribosomes are able to interact with both YidC1 and YidC2. The interaction is stimulated by the presence of a nascent membrane protein substrate and abolished upon deletion of the C-terminal tail, which also abrogates the YidC-dependent membrane insertion of subunit c of the F1F0-ATPase into the membrane. It is concluded that both YidC1 and YidC2 interact with ribosomes, suggesting that the modes of membrane insertion by these membrane insertases are similar.

Original languageEnglish
Pages (from-to)4545-4551
Number of pages7
JournalJournal of Bacteriology
Volume195
Issue number19
DOIs
Publication statusPublished - Oct-2013

Keywords

  • NASCENT CHAIN COMPLEXES
  • ESCHERICHIA-COLI YIDC
  • MITOCHONDRIAL RIBOSOME
  • BACILLUS-SUBTILIS
  • PROTEIN SECRETION
  • SPOIIIJ GENE
  • FAMILY
  • EXPRESSION
  • BACTERIAL
  • PATHWAY

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