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Journal of Bacteriology, June 2000, p. 3111-3116, Vol. 182, No. 11
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Proteolysis of Bacteriophage lambda  CII by Escherichia coli FtsH (HflB)

Yoram Shotland,1,dagger Amir Shifrin,1 Tamar Ziv,2 Dinah Teff,1 Simi Koby,1 Oren Kobiler,1 and Amos B. Oppenheim1,*

Department of Molecular Genetics and Biotechnology, The Hebrew University-Hadassah Medical School, Jerusalem,1 and The Protein Research Center, Department of Biology, The Technion, Haifa,2 Israel

Received 1 June 1999/Accepted 8 March 2000

FtsH (HflB) is a conserved, highly specific, ATP-dependent protease for which a number of substrates are known. The enzyme participates in the phage lambda  lysis-lysogeny decision by degrading the lambda CII transcriptional activator and by its response to inhibition by the lambda  CIII gene product. In order to gain further insight into the mechanism of the enzymatic activity of FtsH (HflB), we identified the peptides generated following proteolysis of the phage lambda  CII protein. It was found that FtsH (HflB) acts as an endopeptidase degrading CII into small peptides with limited amino acid specificity at the cleavage site. beta -Casein, an unstructured substrate, is also degraded by FtsH (HflB), suggesting that protein structure may play a minor role in determining the products of proteolysis. The majority of the peptides produced were 13 to 20 residues long.

* Corresponding author. Mailing address: Department of Molecular Genetics and Biotechnology, The Hebrew University-Hadassah Medical School, P.O.B. 12272, Jerusalem, Israel 91120. Phone: 972-2-6757309. Fax: 972-2-6757308. E-mail: ao{at}cc.huji.ac.il.

dagger Present address: Washington University School of Medicine, Department of Molecular Microbiology, St. Louis, MO 63110-1093.

Journal of Bacteriology, June 2000, p. 3111-3116, Vol. 182, No. 11
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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