MBBPH@dlvh.daresbury.ac.uk (11/07/90)
can anyone direct me to motif(s) found in 'chaperone proteins. brendan hughes. univ. of oxford uk.
BAIROCH%CH.UNIGE.CMU@PUCC.PRINCETON.EDU (Amos Bairoch) (11/07/90)
From: MBBPH@DLVH.DARESBURY.AC.UK
Subject: chaperone proteins
<can anyone direct me to motif(s) found in 'chaperone proteins.
<brendan hughes. univ. of oxford uk.
From current version of PROSITE:
$PS00296; CHAPERONIN
$BEGIN
*************************
* Chaperonins signature *
*************************
Chaperonins[1,2] are proteins implicated in the assembly of oligomeric protein
complexes. Their role seem to be to assist other polypeptides to maintain or
assume conformations which permit their correct assembly into oligomeric
structures. They are found in abundance in chloroplasts, mitochondria and
prokaryotes. They show weak ATPase activity, and form oligomeric complexes.
The proteins known to belong to the chaperonin family are listed below.
- The chloroplast RuBisCO subunit binding-protein alpha chain, which binds
ribulose bisphosphate carboxylase small and large subunits and which is
implicated in the assembly of the enzyme oligomer.
- The mammalian mitochondrial protein P1 (mitonin) whose function is not yet
known.
- The yeast HSP60 protein, a mitochondrial assembly factor.
- The Escherichia coli groEL protein, which is essential for the growth of
the bacteria and the assembly of several bacteriophages.
- The Mycobacterium tuberculosis and leprae 65 Kd antigen, and the heat shock
protein htpA from Coxiella burnetti, which are probable analogues of groEL.
- The Chlamydial 57 Kd hypersensitivity antigen (hypB) [3].
- A hypothetical protein from Synechococcus 6301 adjacent to an ATP synthase
subunits locus.
We chose, as a signature pattern for this group of proteins, a rather well
conserved region of twelve residues.
-Consensus pattern: A-A-x-E-E-x(4)-G(3)
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in SWISS-PROT: NONE.
-Last update: April 1990 / Text revised.
[ 1] Hemmingsen S.M., Woolford C., van der Vies S.M., Tilly K., Dennis D.T.,
Georgopoulos C.P., Hendrix R.W., Ellis R.J.
Nature 333:330-334(1988).
[ 2] Gupta R.S., Picketts D.J., Ahmad S.
Biochem. Biophys. Res. Commun. 163:780-787(1989).