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Review
. 2000 Oct;5(4):267-75.
doi: 10.1379/1466-1268(2000)005<0267:sdpeat>2.0.co;2.

Sec-dependent protein export and the involvement of the molecular chaperone SecB

J Kim  1 , D A Kendall
Affiliations
Review

Sec-dependent protein export and the involvement of the molecular chaperone SecB

J Kim et al. Cell Stress Chaperones. 2000 Oct.
No abstract available

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Figures

Fig 1.
Fig 1.
Schematic representation of protein transport across the inner membrane of E coli. The nascent polypeptide is recognized by cytoplasmic proteins such as SRP or SecB. It is delivered to a protein translocation channel, SecYEG, in the membrane by a high-affinity SRP-FtsY or SecB-SecA interaction. Subsequently, the signal peptide is cleaved by signal peptidase (leader peptidase), and translocation through the channel is finally completed. Translocation of the polypeptide is powered by multiple rounds of ATP hydrolysis by SecA
Fig 2.
Fig 2.
Schematic representation of the SecYEGDFyajC heterohexameric complex. A heterotrimeric complex of SecY, SecE, and SecG forms a heterohexameric complex with another heterotrimer composed of SecD, SecF, and yajC
Fig 3.
Fig 3.
Schematic representation of the sites of interaction in the SecA-SecB-precursor ternary complex. Residues of SecB responsible for SecA-binding interface with the C-terminal 22 aminoacyl residues of SecA. Residues of SecB associated with interactions with the precursor are also shown. Residues of SecB are italicized, and charged residues are in boldface
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