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Genetic dissection of SecA: suppressor mutations against the secY205 translocase defect.
Genes Cells 2000; 5(12):991-9GC

Abstract

BACKGROUND

The driving force for protein translocation across the bacterial plasma membrane is provided by SecA ATPase, which undergoes striking conformational changes characterized by the membrane insertion and deinsertion cycle. This action of SecA requires the membrane-embedded SecYEG complex. Previously, we have identified a cold-sensitive secY mutation (secY205), affecting the most carboxy-terminal cytosolic domain, that did not allow an ATP-dependent insertion of a SecA-preprotein complex. Thus, this mutant provides an excellent system for genetic analysis of the SecY-SecA interaction.

RESULTS

We carried out a systematic isolation of secA mutations that suppressed secY205 cold-sensitivity. A total of 40 independent suppressor mutations were classified into: (i) allele-specific suppressors, acting only against secY205, and (ii) 'super active' suppressors, acting against almost any sec defects. The former class of mutations, presumably with specific effects on the SecY-SecA interaction, clustered in two regions close to the Walker motif A sequences of the two ATP-binding domains. The latter mutations, enhancing general SecA activities, were mostly in or around the minor ATP-binding domain.

CONCLUSIONS

The Walker motif A regions of SecA are important for the SecA-SecY interaction that leads to the SecA conformational changes required for insertion into the SecYEG channel. The minor ATP-binding domain is important for the down-regulation of SecA activities.

Authors+Show Affiliations

Institute for Virus Research, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

11168585

Citation

Matsumoto, G, et al. "Genetic Dissection of SecA: Suppressor Mutations Against the secY205 Translocase Defect." Genes to Cells : Devoted to Molecular & Cellular Mechanisms, vol. 5, no. 12, 2000, pp. 991-9.
Matsumoto G, Nakatogawa H, Mori H, et al. Genetic dissection of SecA: suppressor mutations against the secY205 translocase defect. Genes Cells. 2000;5(12):991-9.
Matsumoto, G., Nakatogawa, H., Mori, H., & Ito, K. (2000). Genetic dissection of SecA: suppressor mutations against the secY205 translocase defect. Genes to Cells : Devoted to Molecular & Cellular Mechanisms, 5(12), pp. 991-9.
Matsumoto G, et al. Genetic Dissection of SecA: Suppressor Mutations Against the secY205 Translocase Defect. Genes Cells. 2000;5(12):991-9. PubMed PMID: 11168585.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Genetic dissection of SecA: suppressor mutations against the secY205 translocase defect. AU - Matsumoto,G, AU - Nakatogawa,H, AU - Mori,H, AU - Ito,K, PY - 2001/2/13/pubmed PY - 2001/4/6/medline PY - 2001/2/13/entrez SP - 991 EP - 9 JF - Genes to cells : devoted to molecular & cellular mechanisms JO - Genes Cells VL - 5 IS - 12 N2 - BACKGROUND: The driving force for protein translocation across the bacterial plasma membrane is provided by SecA ATPase, which undergoes striking conformational changes characterized by the membrane insertion and deinsertion cycle. This action of SecA requires the membrane-embedded SecYEG complex. Previously, we have identified a cold-sensitive secY mutation (secY205), affecting the most carboxy-terminal cytosolic domain, that did not allow an ATP-dependent insertion of a SecA-preprotein complex. Thus, this mutant provides an excellent system for genetic analysis of the SecY-SecA interaction. RESULTS: We carried out a systematic isolation of secA mutations that suppressed secY205 cold-sensitivity. A total of 40 independent suppressor mutations were classified into: (i) allele-specific suppressors, acting only against secY205, and (ii) 'super active' suppressors, acting against almost any sec defects. The former class of mutations, presumably with specific effects on the SecY-SecA interaction, clustered in two regions close to the Walker motif A sequences of the two ATP-binding domains. The latter mutations, enhancing general SecA activities, were mostly in or around the minor ATP-binding domain. CONCLUSIONS: The Walker motif A regions of SecA are important for the SecA-SecY interaction that leads to the SecA conformational changes required for insertion into the SecYEG channel. The minor ATP-binding domain is important for the down-regulation of SecA activities. SN - 1356-9597 UR - https://www.unboundmedicine.com/medline/citation/11168585/Genetic_dissection_of_SecA:_suppressor_mutations_against_the_secY205_translocase_defect_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=1356-9597&date=2000&volume=5&issue=12&spage=991 DB - PRIME DP - Unbound Medicine ER -