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Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40.
J Mol Biol. 2001 May 11; 308(4):795-806.JM

Abstract

Large peptidyl-prolyl cis/trans isomerases (PPIases) are important components of the Hsp90 chaperone complex. In mammalian cells, either Cyp40, FKBP51 or FKBP52 is incorporated into these complexes. It has been suggested that members of this protein family exhibit both prolyl isomerase and chaperone activity. Here we define the structural and functional properties of the three mammalian large PPIases. We find that in all cases two PPIase monomers bind to an Hsp90 dimer. However, the affinities of the PPIases are different with FKBP52 exhibiting the strongest interaction and Cyp40 the weakest. Furthermore, in the mammalian system, in contrast to the yeast system, the catalytic activity of prolyl isomerization corresponds well to that of the respective small PPIases. Interestingly, Cyp40 and FKBP51 are the more potent chaperones. Thus, it seems that both the affinity for Hsp90 and the differences in their chaperone properties, which may reflect their interaction with the non-native protein in the Hsp90 complex, are critical for the selective incorporation of a specific large PPIase.

Authors+Show Affiliations

Institut für Organische Chemie und Biochemie, Technische Universität München, Garching, 85747, Germany.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

11350175

Citation

Pirkl, F, and J Buchner. "Functional Analysis of the Hsp90-associated Human Peptidyl Prolyl Cis/trans Isomerases FKBP51, FKBP52 and Cyp40." Journal of Molecular Biology, vol. 308, no. 4, 2001, pp. 795-806.
Pirkl F, Buchner J. Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40. J Mol Biol. 2001;308(4):795-806.
Pirkl, F., & Buchner, J. (2001). Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40. Journal of Molecular Biology, 308(4), 795-806.
Pirkl F, Buchner J. Functional Analysis of the Hsp90-associated Human Peptidyl Prolyl Cis/trans Isomerases FKBP51, FKBP52 and Cyp40. J Mol Biol. 2001 May 11;308(4):795-806. PubMed PMID: 11350175.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40. AU - Pirkl,F, AU - Buchner,J, PY - 2001/5/15/pubmed PY - 2001/6/8/medline PY - 2001/5/15/entrez SP - 795 EP - 806 JF - Journal of molecular biology JO - J Mol Biol VL - 308 IS - 4 N2 - Large peptidyl-prolyl cis/trans isomerases (PPIases) are important components of the Hsp90 chaperone complex. In mammalian cells, either Cyp40, FKBP51 or FKBP52 is incorporated into these complexes. It has been suggested that members of this protein family exhibit both prolyl isomerase and chaperone activity. Here we define the structural and functional properties of the three mammalian large PPIases. We find that in all cases two PPIase monomers bind to an Hsp90 dimer. However, the affinities of the PPIases are different with FKBP52 exhibiting the strongest interaction and Cyp40 the weakest. Furthermore, in the mammalian system, in contrast to the yeast system, the catalytic activity of prolyl isomerization corresponds well to that of the respective small PPIases. Interestingly, Cyp40 and FKBP51 are the more potent chaperones. Thus, it seems that both the affinity for Hsp90 and the differences in their chaperone properties, which may reflect their interaction with the non-native protein in the Hsp90 complex, are critical for the selective incorporation of a specific large PPIase. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/11350175/Functional_analysis_of_the_Hsp90_associated_human_peptidyl_prolyl_cis/trans_isomerases_FKBP51_FKBP52_and_Cyp40_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(01)94595-4 DB - PRIME DP - Unbound Medicine ER -