Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of Escherichia coli

被引:123
作者
Shotland, Y
Koby, S
Teff, D
Mansur, N
Oren, DA
Tatematsu, K
Tomoyasu, T
Kessel, M
Bukau, B
Ogura, T
Oppenheim, AB
机构
[1] HEBREW UNIV JERUSALEM, HADASSAH MED SCH, DEPT MOL GENET & BIOTECHNOL, IL-91120 JERUSALEM, ISRAEL
[2] HEBREW UNIV JERUSALEM, HADASSAH MED SCH, DEPT MEMBRANE & ULTRASTRUCT RES, IL-91120 JERUSALEM, ISRAEL
[3] KUMAMOTO UNIV, SCH MED, INST MOL EMBRYOL & GENET, DEPT MOL CELL BIOL, KUMAMOTO 860, JAPAN
[4] UNIV HEIDELBERG, ZENTRUM MOL BIOL, D-6900 HEIDELBERG, GERMANY
关键词
D O I
10.1046/j.1365-2958.1997.4231796.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Rapid proteolysis plays an important role in regulation of gene expression. Proteolysis of the phage lambda CII transcriptional activator plays a key role in the lysis-lysogeny decision by phage lambda. Here we demonstrate that the E. coli ATP-dependent protease FtsH, the product of the host ftsH/hflB gene, is responsible for the rapid proteolysis of the CII protein. FtsH was found previously to degrade the heat-shock transcription factor sigma(32). Proteolysis of sigma(32) requires, in vivo, the presence of the DnaK-DnaJ-GrpE chaperone machine. Neither DnaK-DnaJ-GrpE nor GroEL-GroES chaperone machines are required for proteolysis of CII in vivo. Purified FtsH carries out specific ATP-dependent proteolysis of CII in vitro. The degradation of CII is at least 10-fold faster than that of sigma(32). Electron microscopy revealed that purified FtsH forms ring-shaped structures with a diameter of 6-7 nm.
引用
收藏
页码:1303 / 1310
页数:8
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