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GroEL is a
protein which belongs to the
chaperonin family of
molecular chaperones, and is
found in many bacteria. It is
required for the
proper folding...
- mitochondria. The
GroEL/GroES
complex in E. coli is a
Group I
chaperonin and the best
characterized large (~ 1 MDa)
chaperonin complex.
GroEL is a double-ring...
- For example, "
GroEL"
originally stands for "phage
growth defect,
overcome by
mutation in
phage gene E,
large subunit". Hsp10/60 (
GroEL/GroES
complex in...
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uniquely identified by a few
conserved signature indel (CSI) in the HSP60 (
GroEL) protein. In addition, a
number of
bacterial taxa (including Negativicutes...
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structural elements of the
substrate proteins that
GroEL recognizes.
Lorimer has also
shown that
GroEL can
perform work on
substrate protein during allosteric...
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conjunction with
GroEL.
GroES exists as a ring-shaped
oligomer of
between six and
eight identical subunits,
while the 60 kDa
chaperonin (cpn60, or
groEL in bacteria)...
- DnaJ Hsp40 (DNAJ*;
three subfamilies in humans) Co-factor of Hsp70 60 kDa
GroEL, 60kDa
antigen Hsp60 (HSPE)
Involved in
protein folding after its post-translational...
-
conserved signature indels in a
number of
important proteins (viz. DnaK,
GroEL). Of
these two
structurally distinct groups of bacteria,
monoderms are indicated...
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Subject Headings (MeSH)
Leclerque A,
Kleespies RG (April 2008). "16S rRNA-,
GroEL- and MucZ-based ****essment of the
taxonomic position of 'Rickettsiella melolonthae'...
-
function and may ****ist most
globular proteins, for example, the
prokaryotic GroEL/GroES
system of
proteins and the
homologous eukaryotic heat
shock proteins...
