The deletion of Ffh in Escherichia coli induces adverse physiological and morphological changes

被引:0
作者
Dong H.J. [1 ]
Shen X.L. [2 ]
Jiang J.Y. [1 ]
Li Y.Q. [2 ]
机构
[1] Institute of Drug Research, Lunan Pharmaceutical Company
[2] College of Life Science, Zhejiang University
基金
中国国家自然科学基金;
关键词
Escherichia coli; Ffh; Membrane proteins;
D O I
10.1134/S1990747809020093
中图分类号
学科分类号
摘要
The Escherichia coli Ffh protein is homologous to the SRP54 subunit of the eukaryotic signal recognition particle (SRP) that is involved in targeting and translocation of membrane proteins. The functions of Ffh in E. coli were investigated using the mutant with the Ffh deficiency. The mutant showed lower growth rate at 30°C and rapidly lost viability at the non-permissive temperature of 42°C. In addition, the amount of the total membrane proteins decreased sharply in the mutant. The mutant cells cultured at either 30 or 42°C appeared to have an elongated shape as compared to the wild type cells. Transmission electron microscopy revealed that the membrane layer of the mutant cells was thinner than that of the wild type cells. © Pleiades Publishing, Ltd. 2009.
引用
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页码:163 / 167
页数:4
相关论文
共 21 条
  • [1] Schatz G., Dobberstein B., Common Principles of Protein Translocation Across Membranes, Science, 271, pp. 1519-1526, (1996)
  • [2] Bernstein H.D., Poritz M.A., Strub K., Hoben P.J., Brenner S., Walter P., Model for Signal Sequence Recognition from Amino-Acid Sequence of 54K Subunit of Signal Recognition Particle, Nature, 340, pp. 482-486, (1989)
  • [3] Romisch K., Webb J., Herz J., Prehn S., Frank R., Vingron M., Dobberstein B., Homology of 54K Protein of Signal-Recognition Particle, Docking Protein and Two E. coli Proteins with Putative GTP-Binding Domains, Nature, 340, pp. 478-482, (1989)
  • [4] Poritz M.A., Bernstein H.D., Strub K., Zopf D., Wilhelm H., Walter P., An E. coli Ribonucleoprotein Containing 4.5S RNA Resembles Mammalian Signal Recognition Particle, Science, 250, pp. 1111-1117, (1990)
  • [5] Poritz M.A., Strub K., Walter P., Human SRP RNA and E. coli 4.5S RNA Contain a Highly Homologous Structural Domain, Cell, 55, pp. 4-6, (1988)
  • [6] Ribes V., Romisch K., Giner A., Dobberstein B., Tollervey D., E. coli 4.5S RNA Is Part of a Ribonucleoprotein Particle That Has Properties Related to Signal Recognition Particle, Cell, 63, pp. 591-600, (1990)
  • [7] Kumamoto C.A., Beckwith J., Mutations in a New Gene, secB, Cause Defective Protein Localization in Escherichia coli, J. Bacteriol., 154, pp. 253-260, (1983)
  • [8] Oliver D.B., Beckwith J., E. coli Mutant Pleiotropically Defective in the Export of Secreted Proteins, Cell, 25, pp. 765-772, (1981)
  • [9] Schatz P.J., Riggs P.D., Jacq A., Fath M.J., Beckwith J., The secE Gene Encodes an Integral Membrane Protein Required for Protein Export in Escherichia coli, Genes Dev., 3, pp. 1035-1044, (1989)
  • [10] Shiba K., Ito K., Yura T., Ceretti D.P., A Defined Mutation in the Protein Export Gene within the spc Ribosomal Protein Operon of Escherichia coli: Isolation and Characterization of a New Temperature-Sensitive secY Mutation, EMBO J., 3, pp. 631-635, (1984)