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Multiple SecA molecules drive protein translocation across a single translocon with SecG inversion.
J Biol Chem 2012; 287(1):455-64JB

Abstract

SecA is a translocation ATPase that drives protein translocation. D209N SecA, a dominant-negative mutant, binds ATP but is unable to hydrolyze it. This mutant was inactive to proOmpA translocation. However, it generated a translocation intermediate of 18 kDa. Further addition of wild-type SecA caused its translocation into either mature OmpA or another intermediate of 28 kDa that can be translocated into mature by a proton motive force. The addition of excess D209N SecA during translocation caused a topology inversion of SecG. Moreover, an intermediate of SecG inversion was identified when wild-type and D209N SecA were used in the same amounts. These results indicate that multiple SecA molecules drive translocation across a single translocon with SecG inversion. Here, we propose a revised model of proOmpA translocation in which a single catalytic cycle of SecA causes translocation of 10-13 kDa with ATP binding and hydrolysis, and SecG inversion is required when the next SecA cycle begins with additional ATP hydrolysis.

Authors+Show Affiliations

Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo 113-0032, Japan.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22074917

Citation

Morita, Kazuhiro, et al. "Multiple SecA Molecules Drive Protein Translocation Across a Single Translocon With SecG Inversion." The Journal of Biological Chemistry, vol. 287, no. 1, 2012, pp. 455-64.
Morita K, Tokuda H, Nishiyama K. Multiple SecA molecules drive protein translocation across a single translocon with SecG inversion. J Biol Chem. 2012;287(1):455-64.
Morita, K., Tokuda, H., & Nishiyama, K. (2012). Multiple SecA molecules drive protein translocation across a single translocon with SecG inversion. The Journal of Biological Chemistry, 287(1), pp. 455-64. doi:10.1074/jbc.M111.301754.
Morita K, Tokuda H, Nishiyama K. Multiple SecA Molecules Drive Protein Translocation Across a Single Translocon With SecG Inversion. J Biol Chem. 2012 Jan 2;287(1):455-64. PubMed PMID: 22074917.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Multiple SecA molecules drive protein translocation across a single translocon with SecG inversion. AU - Morita,Kazuhiro, AU - Tokuda,Hajime, AU - Nishiyama,Ken-ichi, Y1 - 2011/11/10/ PY - 2011/11/15/entrez PY - 2011/11/15/pubmed PY - 2012/5/9/medline SP - 455 EP - 64 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 287 IS - 1 N2 - SecA is a translocation ATPase that drives protein translocation. D209N SecA, a dominant-negative mutant, binds ATP but is unable to hydrolyze it. This mutant was inactive to proOmpA translocation. However, it generated a translocation intermediate of 18 kDa. Further addition of wild-type SecA caused its translocation into either mature OmpA or another intermediate of 28 kDa that can be translocated into mature by a proton motive force. The addition of excess D209N SecA during translocation caused a topology inversion of SecG. Moreover, an intermediate of SecG inversion was identified when wild-type and D209N SecA were used in the same amounts. These results indicate that multiple SecA molecules drive translocation across a single translocon with SecG inversion. Here, we propose a revised model of proOmpA translocation in which a single catalytic cycle of SecA causes translocation of 10-13 kDa with ATP binding and hydrolysis, and SecG inversion is required when the next SecA cycle begins with additional ATP hydrolysis. SN - 1083-351X UR - https://www.unboundmedicine.com/medline/citation/22074917/Multiple_SecA_molecules_drive_protein_translocation_across_a_single_translocon_with_SecG_inversion_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=22074917 DB - PRIME DP - Unbound Medicine ER -