Substrate Proteins Take Shape at an Improved Bacterial Translocon.
J Bacteriol
; 201(1)2019 01 01.
Article
em En
| MEDLINE
| ID: mdl-30322856
ABSTRACT
Characterization of Sec-dependent bacterial protein transport has often relied on an in vitro protein translocation system comprised in part of Escherichia coli inverted inner membrane vesicles or, more recently, purified SecYEG translocons reconstituted into liposomes using mostly a single substrate (proOmpA). A paper published in this issue (P. Bariya and L. Randall, J Bacteriol 201e00493-18, 2019, https//doi.org/10.1128/JB.00493-18) finds that inclusion of SecA protein during SecYEG proteoliposome reconstitution dramatically improves the number of active translocons. This experimentally useful and intriguing result that may arise from SecA membrane integration properties is discussed here. Furthermore, determination of the rate-limiting transport step for nine different substrates implicates the mature region distal to the signal peptide in the observed rate constant differences, indicating that more nuanced transport models that respond to differences in protein sequence and structure are needed.
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MEDLINE
Assunto principal:
Proteínas de Escherichia coli
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article