April 21, 2020  |  

Membrane proteomic analysis reveals overlapping and independent functions of Streptococcus mutans Ffh, YidC1, and YidC2.

Authors: Mishra, Surabhi and Crowley, Paula J and Wright, Katherine R and Palmer, Sara R and Walker, Alejandro R and Datta, Susmita and Brady, L Jeannine

A comparative proteomic analysis was utilized to evaluate similarities and differences in membrane samples derived from the cariogenic bacterium Streptococcus mutans, including the wild-type strain and four mutants devoid of protein translocation machinery components, specifically ?ffh, ?yidC1, ?yidC2, or ?ffh/yidC1. The purpose of this work was to determine the extent to which the encoded proteins operate individually or in concert with one another and to identify the potential substrates of the respective pathways. Ffh is the principal protein component of the signal recognition particle (SRP), while yidC1 and yidC2 are dual paralogs encoding members of the YidC/Oxa/Alb family of membrane-localized chaperone insertases. Our results suggest that the co-translational SRP pathway works in concert with either YidC1 or YidC2 specifically, or with no preference for paralog, in the insertion of most membrane-localized substrates. A few instances were identified in which the SRP pathway alone, or one of the YidCs alone, appeared to be most relevant. These data shed light on underlying reasons for differing phenotypic consequences of ffh, yidC1 or yidC2 deletion. Our data further suggest that many membrane proteins present in a ?yidC2 background may be non-functional, that ?yidC1 is better able to adapt physiologically to the loss of this paralog, that shared phenotypic properties of ?ffh and ?yidC2 mutants can stem from impacts on different proteins, and that independent binding to ribosomal proteins is not a primary functional activity of YidC2. Lastly, genomic mutations accumulate in a ?yidC2 background coincident with phenotypic reversion, including an apparent W138R suppressor mutation within yidC1. © 2019 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.

Journal: Molecular oral microbiology
DOI: 10.1111/omi.12261
Year: 2019

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