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Determinants of the quantity of the stable SecY complex in the Escherichia coli cell.
J Bacteriol 1993; 175(24):7771-5JB

Abstract

While SecY in wild-type Escherichia coli cells is stable and is complexed with other proteins within the membrane, moderately overexpressed and presumably uncomplexed SecY was degraded with a half-life of 2 min. The fact that the amount of stable SecY is strictly regulated by the degradation of excess SecY was demonstrated by competitive entry of the SecY+ protein and a SecY-LacZ alpha fusion protein into the stable pool. Simultaneous overexpression of SecE led to complete stabilization of excess SecY. Overproduced SecD and SecF did not affect the stability of SecY, but plasmids carrying ORF12 located within the secD-secF operon partially stabilized this protein. In contrast, mutational reduction of the SecE content (but not the ORF12 content) led to the appearance of two populations of newly synthesized SecY molecules, one that was immediately degraded and one that was completely stable. Thus, the E. coli cell is equipped with a system that eliminates SecY unless it is complexed with SecE, a limiting partner of SecY. Our observations implied that in wild-type cells, SecY and SecE rapidly associate with each other and remain complexed.

Authors+Show Affiliations

Department of Cell Biology, Kyoto University, 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

8253665

Citation

Taura, T, et al. "Determinants of the Quantity of the Stable SecY Complex in the Escherichia Coli Cell." Journal of Bacteriology, vol. 175, no. 24, 1993, pp. 7771-5.
Taura T, Baba T, Akiyama Y, et al. Determinants of the quantity of the stable SecY complex in the Escherichia coli cell. J Bacteriol. 1993;175(24):7771-5.
Taura, T., Baba, T., Akiyama, Y., & Ito, K. (1993). Determinants of the quantity of the stable SecY complex in the Escherichia coli cell. Journal of Bacteriology, 175(24), pp. 7771-5.
Taura T, et al. Determinants of the Quantity of the Stable SecY Complex in the Escherichia Coli Cell. J Bacteriol. 1993;175(24):7771-5. PubMed PMID: 8253665.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Determinants of the quantity of the stable SecY complex in the Escherichia coli cell. AU - Taura,T, AU - Baba,T, AU - Akiyama,Y, AU - Ito,K, PY - 1993/12/1/pubmed PY - 1993/12/1/medline PY - 1993/12/1/entrez SP - 7771 EP - 5 JF - Journal of bacteriology JO - J. Bacteriol. VL - 175 IS - 24 N2 - While SecY in wild-type Escherichia coli cells is stable and is complexed with other proteins within the membrane, moderately overexpressed and presumably uncomplexed SecY was degraded with a half-life of 2 min. The fact that the amount of stable SecY is strictly regulated by the degradation of excess SecY was demonstrated by competitive entry of the SecY+ protein and a SecY-LacZ alpha fusion protein into the stable pool. Simultaneous overexpression of SecE led to complete stabilization of excess SecY. Overproduced SecD and SecF did not affect the stability of SecY, but plasmids carrying ORF12 located within the secD-secF operon partially stabilized this protein. In contrast, mutational reduction of the SecE content (but not the ORF12 content) led to the appearance of two populations of newly synthesized SecY molecules, one that was immediately degraded and one that was completely stable. Thus, the E. coli cell is equipped with a system that eliminates SecY unless it is complexed with SecE, a limiting partner of SecY. Our observations implied that in wild-type cells, SecY and SecE rapidly associate with each other and remain complexed. SN - 0021-9193 UR - https://www.unboundmedicine.com/medline/citation/8253665/Determinants_of_the_quantity_of_the_stable_SecY_complex_in_the_Escherichia_coli_cell_ L2 - http://jb.asm.org/cgi/pmidlookup?view=long&pmid=8253665 DB - PRIME DP - Unbound Medicine ER -