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PMID: 10809689 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Proteolysis of bacteriophage lambda CII by Escherichia coli FtsH (HflB).

Journal of bacteriology ·Vol. 182 ·No. 11 ·2000-06-00 ·Pages 3111-6

Shotland Y, Shifrin A, Ziv T, Teff D, Koby S, Kobiler O, Oppenheim AB

Abstract

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.

MeSH Terms
ATP-Dependent Proteases Amino Acid Sequence Bacterial Proteins/metabolism Bacteriophage lambda Caseins/metabolism Endopeptidases/metabolism Escherichia coli/enzymology Escherichia coli Proteins Membrane Proteins/metabolism Metalloendopeptidases/metabolism Molecular Sequence Data Substrate Specificity Transcription Factors/isolation & purification,metabolism Viral Proteins
Chemicals
Bacterial Proteins Caseins Escherichia coli Proteins Membrane Proteins Transcription Factors Viral Proteins cII protein, bacteriophage lambda Endopeptidases ATP-Dependent Proteases FtsH protein, E coli Metalloendopeptidases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Shotland Y
Department of Molecular Genetics and Biotechnology, The Hebrew University-Hadassah Medical School, Jerusalem, Israel.
Shifrin A
Ziv T
Teff D
Koby S
Kobiler O
Oppenheim A B
References (35)
35 references, click to expand
  1. Lambda Xis degradation in vivo by Lon and FtsH.
    J Bacteriol. 1998 Mar;180(6):1573-7 PMID: 9515930
  2. The proteasome: paradigm of a self-compartmentalizing protease.
    Cell. 1998 Feb 6;92(3):367-80 PMID: 9476896
  3. Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease.
    Cell. 1998 Jun 12;93(6):973-83 PMID: 9635427
  4. Different pathways for protein degradation by the FtsH/HflKC membrane-embedded protease complex: an implication from the interference by a mutant form of a new substrate protein, YccA.
    J Mol Biol. 1998 May 29;279(1):175-88 PMID: 9636708
  5. Nuclear power and mitochondrial disease.
    Nat Genet. 1998 Jul;19(3):214-5 PMID: 9662387
  6. Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein.
    Cell. 1998 Aug 21;94(4):525-36 PMID: 9727495
  7. Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP.
    Nat Struct Biol. 1998 Sep;5(9):803-11 PMID: 9731775
  8. Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli.
    Mol Microbiol. 1999 Feb;31(3):833-44 PMID: 10048027
  9. Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease.
    Nature. 1999 Mar 25;398(6725):348-51 PMID: 10192337
  10. Protein quality control: triage by chaperones and proteases.
    Genes Dev. 1997 Apr 1;11(7):815-23 PMID: 9106654
  11. Control of phage lambda development by stability and synthesis of cII protein: role of the viral cIII and host hflA, himA and himD genes.
    Cell. 1982 Dec;31(3 Pt 2):565-73 PMID: 6218885
  12. Control of bacteriophage lambda CII activity by bacteriophage and host functions.
    J Bacteriol. 1984 Jul;159(1):238-42 PMID: 6330032
  13. Translational regulatory signals within the coding region of the bacteriophage lambda cIII gene.
    J Bacteriol. 1986 Jul;167(1):415-9 PMID: 2941413
  14. Genetic analysis of bacteriophage lambda cIII gene: mRNA structural requirements for translation initiation.
    J Bacteriol. 1989 May;171(5):2563-72 PMID: 2523380
  15. Primary and predicted secondary structures of the caseins in relation to their biological functions.
    Protein Eng. 1988 Oct;2(4):251-9 PMID: 3074304
  16. Use of T7 RNA polymerase to direct expression of cloned genes.
    Methods Enzymol. 1990;185:60-89 PMID: 2199796
  17. The activity of the CIII regulator of lambdoid bacteriophages resides within a 24-amino acid protein domain.
    Proc Natl Acad Sci U S A. 1991 Jun 15;88(12):5217-21 PMID: 1828895
  18. Escherichia coli mutant Y16 is a double mutant carrying thermosensitive ftsH and ftsI mutations.
    J Bacteriol. 1992 Apr;174(7):2416-7 PMID: 1551860
  19. The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression.
    J Bacteriol. 1993 Mar;175(5):1344-51 PMID: 8444796
  20. Involvement of FtsH in protein assembly into and through the membrane. II. Dominant mutations affecting FtsH functions.
    J Biol Chem. 1994 Feb 18;269(7):5225-9 PMID: 8106505
  21. Existence of a molecular ruler in proteasomes suggested by analysis of degradation products.
    FEBS Lett. 1994 Aug 1;349(2):205-9 PMID: 8050567
  22. Degradation of sigma 32, the heat shock regulator in Escherichia coli, is governed by HflB.
    Proc Natl Acad Sci U S A. 1995 Apr 11;92(8):3516-20 PMID: 7724592
  23. Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32.
    EMBO J. 1995 Jun 1;14(11):2551-60 PMID: 7781608
  24. A 200-amino acid ATPase module in search of a basic function.
    Bioessays. 1995 Jul;17(7):639-50 PMID: 7646486
  25. FtsH, a membrane-bound ATPase, forms a complex in the cytoplasmic membrane of Escherichia coli.
    J Biol Chem. 1995 Oct 6;270(40):23485-90 PMID: 7559511
  26. The tolZ gene of Escherichia coli is identified as the ftsH gene.
    J Bacteriol. 1996 Jun;178(12):3457-61 PMID: 8655541
  27. The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria.
    Cell. 1996 Jun 14;85(6):875-85 PMID: 8681382
  28. Subunit a of proton ATPase F0 sector is a substrate of the FtsH protease in Escherichia coli.
    FEBS Lett. 1996 Dec 9;399(1-2):26-8 PMID: 8980112
  29. Proteases and their targets in Escherichia coli.
    Annu Rev Genet. 1996;30:465-506 PMID: 8982462
  30. Host regulation of lysogenic decision in bacteriophage lambda: transmembrane modulation of FtsH (HflB), the cII degrading protease, by HflKC (HflA).
    Proc Natl Acad Sci U S A. 1997 May 27;94(11):5544-9 PMID: 9159109
  31. Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of Escherichia coli.
    Mol Microbiol. 1997 Jun;24(6):1303-10 PMID: 9218777
  32. Sequence analysis of the AAA protein family.
    Protein Sci. 1997 Oct;6(10):2043-58 PMID: 9336829
  33. Self-compartmentalizing proteases.
    Trends Biochem Sci. 1997 Oct;22(10):399-404 PMID: 9357316
  34. Regulatory subunits of energy-dependent proteases.
    Cell. 1997 Nov 14;91(4):435-8 PMID: 9390551
  35. Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH).
    Genes Dev. 1998 May 1;12(9):1348-55 PMID: 9573051
Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/JB.182.11.3111-3116.2000
Published
2000-06-00
Pages
3111-6
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC94496
Subset
IM
External Links
PubMed source DOI: 10.1128/JB.182.11.3111-3116.2000 PMC Full Text View journal details
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