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Wheat FKBP73 functions in vitro as a molecular chaperone independently of its peptidyl prolyl cis-trans isomerase activity.
Planta. 2002 May; 215(1):119-26.P

Abstract

Peptidyl-prolyl cis-trans isomerases (PPIases) catalyse protein folding by accelerating the slow step of cis-trans isomerisation of peptidyl-prolyl bonds. Wheat (Triticum aestivum L.) FKBP73 (wFKBP73) is a peptidyl-prolyl cis-trans isomerase belonging to the FK506-binding protein (FKBP) family. It comprises three FKBP12-like domains, tetratricopeptide repeats and a calmodulin-binding domain (CaMbd). In vitro studies indicated that wFKBP73 possesses PPIase activity, binds calmodulin and forms a heterocomplex with mammalian p23 and wheat Hsp90 in wheat-germ lysate. To further study the role of wFKBP73 we have analysed its chaperone properties. Using the thermal unfolding and aggregation of citrate synthase (CS) as a model system, we have shown that the plant wFKBP73 exhibits chaperone activity, being able to suppress CS aggregation independently of its PPIase activity. The wFKBP73 interacts transiently with non-native CS and slows down its inactivation kinetics, whereas the mammalian homologue, hFKBP52 binds tightly to CS and does not affect its rate of inactivation. Hence, the first plant FKBP shown to function as a molecular chaperone has a mode of action different from that of the mammalian FKBP52.

Authors+Show Affiliations

Dep[artment of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel. adina@post.tau.ac.ilNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

12012248

Citation

Kurek, Isaac, et al. "Wheat FKBP73 Functions in Vitro as a Molecular Chaperone Independently of Its Peptidyl Prolyl Cis-trans Isomerase Activity." Planta, vol. 215, no. 1, 2002, pp. 119-26.
Kurek I, Pirkl F, Fischer E, et al. Wheat FKBP73 functions in vitro as a molecular chaperone independently of its peptidyl prolyl cis-trans isomerase activity. Planta. 2002;215(1):119-26.
Kurek, I., Pirkl, F., Fischer, E., Buchner, J., & Breiman, A. (2002). Wheat FKBP73 functions in vitro as a molecular chaperone independently of its peptidyl prolyl cis-trans isomerase activity. Planta, 215(1), 119-26.
Kurek I, et al. Wheat FKBP73 Functions in Vitro as a Molecular Chaperone Independently of Its Peptidyl Prolyl Cis-trans Isomerase Activity. Planta. 2002;215(1):119-26. PubMed PMID: 12012248.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Wheat FKBP73 functions in vitro as a molecular chaperone independently of its peptidyl prolyl cis-trans isomerase activity. AU - Kurek,Isaac, AU - Pirkl,Franziska, AU - Fischer,Elke, AU - Buchner,Johannes, AU - Breiman,Adina, Y1 - 2002/02/01/ PY - 2001/07/24/received PY - 2001/10/05/accepted PY - 2002/5/16/pubmed PY - 2002/8/24/medline PY - 2002/5/16/entrez SP - 119 EP - 26 JF - Planta JO - Planta VL - 215 IS - 1 N2 - Peptidyl-prolyl cis-trans isomerases (PPIases) catalyse protein folding by accelerating the slow step of cis-trans isomerisation of peptidyl-prolyl bonds. Wheat (Triticum aestivum L.) FKBP73 (wFKBP73) is a peptidyl-prolyl cis-trans isomerase belonging to the FK506-binding protein (FKBP) family. It comprises three FKBP12-like domains, tetratricopeptide repeats and a calmodulin-binding domain (CaMbd). In vitro studies indicated that wFKBP73 possesses PPIase activity, binds calmodulin and forms a heterocomplex with mammalian p23 and wheat Hsp90 in wheat-germ lysate. To further study the role of wFKBP73 we have analysed its chaperone properties. Using the thermal unfolding and aggregation of citrate synthase (CS) as a model system, we have shown that the plant wFKBP73 exhibits chaperone activity, being able to suppress CS aggregation independently of its PPIase activity. The wFKBP73 interacts transiently with non-native CS and slows down its inactivation kinetics, whereas the mammalian homologue, hFKBP52 binds tightly to CS and does not affect its rate of inactivation. Hence, the first plant FKBP shown to function as a molecular chaperone has a mode of action different from that of the mammalian FKBP52. SN - 0032-0935 UR - https://www.unboundmedicine.com/medline/citation/12012248/Wheat_FKBP73_functions_in_vitro_as_a_molecular_chaperone_independently_of_its_peptidyl_prolyl_cis_trans_isomerase_activity_ L2 - https://dx.doi.org/10.1007/s00425-001-0722-0 DB - PRIME DP - Unbound Medicine ER -