PMID- 10843850
OWN - NLM
STAT- MEDLINE
DCOM- 20000712
LR  - 20101008
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 299
IP  - 4
DP  - 2000 Jun 16
TI  - Characterization of a conserved alpha-helical, coiled-coil motif at the 
      C-terminal domain of the ATP-dependent FtsH (HflB) protease of Escherichia coli.
PG  - 953-64
AB  - FtsH (HflB) is an ATP-dependent protease found in prokaryotic cells, mitochondria 
      and chloroplasts. Here, we have identified, in the carboxy-terminal region of 
      FtsH (HfIB), a short alpha helix predicted of forming a coiled-coil, leucine 
      zipper, structure. This region appears to be structurally conserved. The presence 
      of the coiled-coil motif in the Escherichia coli FtsH (HflB) was demonstrated by 
      circular dichroism and cross-linking experiments. Mutational analysis showed that 
      three highly conserved leucine residues are essential for FtsH (HfIB) activity in 
      vivo and in vitro. Purified proteins mutated in the conserved leucine residues, 
      were found to be defective in the degradation of E. coli sigma(32) and the 
      bacteriophage lambda CII proteins. In addition, the mutant proteins were 
      defective in the binding of CII The mutations did not interfere with the ATPase 
      activity of FtsH (HflB). Finally, the mutant proteins were found to be more 
      sensitive to trypsin degradation than the wild-type enzyme suggesting that the 
      alpha helical region is an important structural element of FtsH (HflB).
CI  - Copyright 2000 Academic Press.
FAU - Shotland, Y
AU  - Shotland Y
AD  - Department of Molecular Genetics and Biotechnology, The Hebrew 
      University-Hadassah Medical School, Jerusalem, P.O. Box 12272, Israel.
FAU - Teff, D
AU  - Teff D
FAU - Koby, S
AU  - Koby S
FAU - Kobiler, O
AU  - Kobiler O
FAU - Oppenheim, A B
AU  - Oppenheim AB
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (Bacterial Proteins)
RN  - 0 (Cross-Linking Reagents)
RN  - 0 (Escherichia coli Proteins)
RN  - 0 (Heat-Shock Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Sigma Factor)
RN  - 0 (Transcription Factors)
RN  - 0 (Viral Proteins)
RN  - 0 (cII protein, bacteriophage lambda)
RN  - 0 (heat-shock sigma factor 32)
RN  - EC 3.4.21.- (ATP-Dependent Proteases)
RN  - EC 3.4.21.- (FtsH protein, E coli)
RN  - EC 3.4.21.4 (Trypsin)
RN  - EC 3.6.1.- (Adenosine Triphosphatases)
SB  - IM
MH  - ATP-Dependent Proteases
MH  - Adenosine Triphosphatases/chemistry/genetics/isolation & purification/metabolism
MH  - Amino Acid Motifs
MH  - Amino Acid Sequence
MH  - Bacterial Proteins/*chemistry/genetics/isolation & purification/metabolism
MH  - Circular Dichroism
MH  - Conserved Sequence/genetics
MH  - Cross-Linking Reagents/metabolism
MH  - Escherichia coli/*enzymology/genetics
MH  - Escherichia coli Proteins
MH  - Heat-Shock Proteins/metabolism
MH  - Membrane Proteins/*chemistry/genetics/isolation & purification/metabolism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Mutation/genetics
MH  - Peptide Fragments/chemistry/metabolism
MH  - Protein Binding
MH  - Protein Structure, Secondary
MH  - Protein Structure, Tertiary
MH  - Recombinant Fusion Proteins/chemistry/genetics/isolation & 
      purification/metabolism
MH  - Sequence Alignment
MH  - *Sigma Factor
MH  - Transcription Factors/metabolism
MH  - Trypsin/metabolism
MH  - Viral Proteins
EDAT- 2000/06/14 09:00
MHDA- 2000/07/15 11:00
CRDT- 2000/06/14 09:00
PHST- 2000/06/14 09:00 [pubmed]
PHST- 2000/07/15 11:00 [medline]
PHST- 2000/06/14 09:00 [entrez]
AID - S0022-2836(00)93767-7 [pii]
AID - 10.1006/jmbi.2000.3767 [doi]
PST - ppublish
SO  - J Mol Biol. 2000 Jun 16;299(4):953-64. doi: 10.1006/jmbi.2000.3767.