GrpE (Gro-P like protein E) is a bacterial nucleotide exchange factor that is important for regulation of protein folding machinery, as well as the heat shock response.[1] It is a heat-inducible protein and during stress it prevents unfolded proteins from accumulating in the cytoplasm.[2][3] Accumulation of unfolded proteins in the cytoplasm can lead to cell death.[4]
| GrpE Protein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Crystal structure of GrpE homodimer interacting with ATPase binding site of DnaK, resolved at 2.8 angstrom. | |||||||||
| Identifiers | |||||||||
| Symbol | GrpE | ||||||||
| Pfam | PF01025 | ||||||||
| InterPro | IPR000740 | ||||||||
| PROSITE | PS01071 | ||||||||
| SCOP2 | 1dkg / SCOPe / SUPFAM | ||||||||
| CDD | cd00446 | ||||||||
| |||||||||
- ^ Delaney JM. A grpE mutant of Escherichia coli is more resistant to heat than the wild-type. J Gen Microbiol. 1990;136(5):797-801. doi:10.1099/00221287-136-5-797
- ^ Bracher A, Verghese J (2015-04-07). "The nucleotide exchange factors of Hsp70 molecular chaperones". Frontiers in Molecular Biosciences. 2: 10. doi:10.3389/fmolb.2015.00010. PMC 4753570. PMID 26913285.
- ^ Harrison C (2003). "GrpE, a nucleotide exchange factor for DnaK". Cell Stress & Chaperones. 8 (3): 218–24. PMC 514874. PMID 14984054.
- ^ Richter K, Haslbeck M, Buchner J (October 2010). "The heat shock response: life on the verge of death". Molecular Cell. 40 (2): 253–66. doi:10.1016/j.molcel.2010.10.006. PMID 20965420.