SecA Cotranslationally Interacts with Nascent Substrate Proteins In Vivo

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 2016 Nov 1

PMID 27795329

Citations 35

Authors

Damon Huber

Mohammed Jamshad

Ruby Hanmer

Daniela Schibich

Kristina Doring

Isabella Marcomini

Gunter Kramer

Bernd Bukau

Affiliations

Soon will be listed here.

Abstract

Importance: SecA is an ATPase that provides the energy for the translocation of proteins across the cytoplasmic membrane by the Sec machinery in bacteria. The translocation of most of these proteins is uncoupled from protein synthesis and is frequently described as "posttranslational." Here, we show that SecA interacts with nascent Sec substrates. This interaction is not dependent on SecB or trigger factor, which also interact with nascent Sec substrates. Moreover, the interaction of SecB with nascent polypeptides is dependent on the interaction of SecA with the ribosome, suggesting that interaction of the nascent chain with SecA precedes interaction with SecB. Our results suggest that SecA could recognize substrate proteins cotranslationally in order to efficiently target them for uncoupled protein translocation.

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