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The role of the DIF motif of the DnaJ (Hsp40) co-chaperone in the regulation of the DnaK (Hsp70) chaperone cycle

Horne, B. E.
Georgopoulos, Costa Panos
Published in The Journal of biological chemistry. 2006, vol. 281, no. 18, p. 12436-12444
Abstract To perform effectively as a molecular chaperone, DnaK (Hsp70) necessitates the assistance of its DnaJ (Hsp40) co-chaperone partner, which efficiently stimulates its intrinsically weak ATPase activity and facilitates its interaction with polypeptide substrates. In this study, we address the function of the conserved glycine- and phenylalanine-rich (G/F-rich) region of the Escherichia coli DnaJ in the DnaK chaperone cycle. We show that the G/F-rich region is critical for DnaJ co-chaperone functions in vivo and that despite a significant degree of sequence conservation among the G/F-rich regions of Hsp40 homologs from bacteria, yeast, or humans, functional complementation in the context of the E. coli DnaJ is limited. Furthermore, we found that the deletion of the whole G/F-rich region is mirrored by mutations in the conserved Asp-Ile/Val-Phe (DIF) motif contained in this region. Further genetic and biochemical analyses revealed that this amino acid triplet plays a critical role in regulation of the DnaK chaperone cycle, possibly by modulating a crucial step subsequent to DnaK-mediated ATP hydrolysis.
Keywords Adenosine Triphosphate/chemistryAmino Acid MotifsAmino Acid SequenceAnimalsConserved SequenceEscherichia coli/metabolismEscherichia coli Proteins/ chemistry/metabolismGlycine/chemistryHSP40 Heat-Shock Proteins/ chemistry/metabolismHSP70 Heat-Shock Proteins/ chemistry/metabolismHumansHydrolysisMolecular Chaperones/chemistryMolecular Sequence DataPhenylalanine/chemistry
PMID: 16533811
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Other version: http://www.jbc.org/content/281/18/12436.full.pdf
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COGELJA CAJO, Gordana et al. The role of the DIF motif of the DnaJ (Hsp40) co-chaperone in the regulation of the DnaK (Hsp70) chaperone cycle. In: The Journal of biological chemistry, 2006, vol. 281, n° 18, p. 12436-12444. doi: 10.1074/jbc.M511192200 https://archive-ouverte.unige.ch/unige:7128

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Deposited on : 2010-06-21

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