Disease relevance of groES

• Using five T-cell clones from two leprosy patients as probes, expression of the M. leprae GroES protein in Escherichia coli after heat shock was demonstrated [1].
• The Mycobacterium tuberculosis BCG-a protein has homology with the Escherichia coli GroES protein [2].
• In order to obtain information on the structural stability and unfolding-refolding mechanism of GroES protein, especially at protein concentrations (0.4-1.2 mM GroES monomer) that would mimic heat stress conditions in vivo, we have performed synchrotron small-angle X-ray scattering (SAXS) experiments [3].

High impact information on groES

• Both gel filtration on an AcA34 sizing column and glycerol gradient centrifugation indicate that the groES protein possesses an oligomeric structure of Mr 80,000 [4].
• The Mr 15,000 groES protein was overproduced and purified to homogeneity by monitoring its presence after polyacrylamide gel electrophoresis [4].
• This unfolding transition curve as well as the refolding kinetics were dependent on the concentration of GroES protein [5].
• The refolding of GroES protein from 3 M Gdn-HCl was probed functionally by measuring the extent of inhibition of GroEL ATPase activity and the enhancement of lactate dehydrogenase refolding yields in the presence of GroEL and ADP [5].
• Cross-reactions with Chlamydia pneumoniae or Escherichia coli GroES protein are limited but may occur [6].

Physical interactions of groES

• Recently, we have identified a region of the GroES protein that interacts with the GroEL protein [7].

Analytical, diagnostic and therapeutic context of groES

• V. harveyi GroES protein had a lower molecular mass (14.5 kDa) than E. coli GroES, migrating in SDS-PAGE as 15kDa protein [8].

References