GroEL

Case study 1: Ayako Endo, 2006

The researchers investigated a temperature adaptation of Bacillus subtilis 168 in which chromosomal groEL was replaced with a psychrophilic groEL. This strain can grow at 50 degrees C but not at 51 degrees C, a temperature at which wild-type B. subtilis can grow. Using in vivo random mutagenesis by the B. subtilis mutator strain (mutS, mutM, mutY), two thermo-adaptants were isolated from the groEL substituted strain at 52 degrees C. They contained novel amino acid alterations in their ATP binding motif (T93I) and the inter-monomer contact (R285H) region of GroEL. These results suggest that GroEL participates in bacterial temperature adaptation.

Fig1. Western blot analysis of groEL expression at 37 °C (A) and 50 °C (B).

Fig2. Growth curves of Thermo-Adaptated groEL strains.

Case study 2: F Edenhofer, 1996

Prions mediate the pathogenesis of certain neurodegenerative diseases, including bovine spongiform encephalopathy in cattle and Creutzfeldt-Jakob disease in humans. The prion particle consists mainly, if not entirely, of PrPSc, a posttranslationally modified isoform of the cellular host-encoded prion protein (PrPc). Here the researchers employ a Saccharomyces cerevisiae two-hybrid screen to search for proteins which interact specifically with the Syrian golden hamster prion protein. The specificity of the interaction was confirmed in vitro for the recombinant proteins PrPc23-231 and rPrP27-30 fused to glutathione S-transferase with recombinant human Hsp60 as well as the bacterial GroEL. The interaction site for recombinant Hsp60 and GroEL proteins was mapped between amino acids 180 and 210 of the prion protein by screening with a set of recombinant PrPc fragments. The binding of Hsp60 and GroEL occurs within a region which contains parts of the putative alpha-helical domains H3 and H4 of the prion protein.

Fig3. Recombinant GST (1 μg) and GST-PrPc (2 μg) immobilized on glutathione-Sepharose as well as glutathione-Sepharose alone were incubated with 25 mg GroEL.

Fig4. Mapping analysis of PrP-GroEL interaction site. The fragments (2 μg each) bound to glutathione Sepharose were incubated with 10 μg of GroEL.

GroEL involved in several pathways and played different roles in them. We selected most pathways GroEL participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with GroEL were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

GroEL has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by GroEL itself. We selected most functions GroEL had, and list some proteins which have the same functions with GroEL. You can find most of the proteins on our site.

GroEL has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with GroEL here. Most of them are supplied by our site. Hope this information will be useful for your research of GroEL.