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The mammalian heat shock protein binding immunophilin (p59/HBI) is an ATP and GTP binding protein.

Abstract：

:A protein of M(r) 59,000 (p59) was recently cloned and identified as a Heat shock protein Binding Immunophilin (p59/HBI). It participates to the heterooligomeric, non-DNA binding form of steroid receptors, in association with the heat shock protein of M(r) 90,000 (hsp90). It binds the immunosuppressants FK506 and rapamycin and possesses three FKBP-12 (FK506 binding protein of M(r) 12,000)--like domains (I to III), plus a tail containing a putative calmodulin binding site (domain IV). Following expression in E. Coli and purification on Glutathione-Sepharose of either the full-length recombinant p59/HBI, or the recombinant FKBP-like domains, we demonstrate by autoradiography of [alpha 32P]-8-azido ATP and of [alpha 32P]-8-azido GTP photoaffinity labeled complexes, that an ATP (GTP) binding site is located in the domain II. This nucleotide binding property is also found with the highly purified rabbit uterus p59/HBI. The latter, but not the recombinant protein, can be phosphorylated in vitro in the presence of Mn++ and/or of Ca++/Calmodulin in an ATP but not GTP dependent manner, suggesting copurification of a CaM kinase II-like enzyme. Thus it appears that p59/HBI is a multifunctional immunophilin which may be at the crossroad of the endocrine and immunological systems.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Le Bihan S,Renoir JM,Radanyi C,Chambraud B,Joulin V,Catelli MG,Baulieu EE

doi

10.1006/bbrc.1993.2088

subject

Has Abstract

pub_date

1993-09-15 00:00:00

pages

600-7

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006291X83720887

journal_volume

195

pub_type

杂志文章

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