P59, an hsp 90-binding protein. Cloning and sequencing of its cDNA and preparation of a peptide-directed polyclonal antibody.

Lebeau, Marie‐Claire; Massol, Nelly; Herrick, Jason R.; Faber, Lee E.; Renoir, Jack‐Michel; Radanyi, Christine; Baulieu, Étienne-Émile

doi:10.1016/s0021-9258(18)42827-x

Cited by 170 publications

(20 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Recently, the same protein was isolated and characterized as an immunophilin following FK506 affinity chromatography (Yem et al, 1992); specific peptide sequences within this protein were shown to have strong homology to FKBP-12 and FKBP-13. The cloning of hsp56 from rabbit liver cDNA was subsequently reported, and the derived amino acid sequence of hsp56 confirmed our original inference that hsp56 contained an FK506-binding domain (Lebeau et al, 1992). Additionally, a human form of hsp56 has now been cloned and expressed in Escherichia coli (Peattie et al, 1992).…”

mentioning

confidence: 55%

“…rabbit (Lebeau et al, 1992) and human (Peattie et al, 1992) hsp56, as shown in Figure 4. In fact, the high level of similarity of these peptides from chicken hsp56 to corresponding peptides from the mammalian proteins made the alignment simple and unambiguous.…”

Section: Resultsmentioning

confidence: 99%

“…0006-2960/93/0432-12571 $04.00/0 We2 and others (Callebaut et al, 1992;Tai et al, 1992;Trandinh et al, 1992) have examined the primary structure of mammalian hsp56 for the presence of domains within the polypeptide, with special emphasis on regions which might show homology to known FK506-binding proteins such as FKBP-12 (Harding et al, 1989;Siekierka et al, 1989;Standaert et al, 1990), FKBP-13 (Jin et al, 1991), and (Galat et al, 1992;Jin et al, 1992). A region with clear homology to FKBP-12, one we have designated FK506-binding domain I, is located near the N-terminus of hsp56, comprising residues 31-135 of the 59-kDa protein (Lebeau et al, 1992;Callebaut et al, 1992;Tai et al, 1992). In fact, this domain is roughly 50% identical in sequence to FKBP-12 and FKBP-13 (Callebaut et al, 1992;Tai et al, 1992).…”

mentioning

confidence: 99%

See 2 more Smart Citations

An active FK506-binding domain of 17,000 daltons is isolated following limited proteolysis of chicken thymus HSP56

Yem¹,

Reardon²,

Leone³

et al. 1993

Biochemistry

View full text Add to dashboard Cite

We have previously identified hsp56, a protein component of steroid receptor complexes, as an FK506 binding protein [Yem et al. (1992) J. Biol. Chem. 267, 2868-2871]. We now report that hsp56 is also found to be a major immunophilin in chicken thymus, by virtue of binding to FK506-Affi-Gel-10 as well as positive cross-reactivity with a polyclonal antiserum directed against human hsp56. Limited digests of purified chicken hsp56 with endoproteinase Lys C result in the production of a unique polypeptide having a mass of about 17 kDa (p17), as judged by Western blotting. Peptide mapping provided additional proof that p17 is a fragment which comprises the entire FK506 binding domain I of chicken hsp56, terminating with an Arg-Lys which might represent a processing site. Binding of radiolabeled dihydro FK506 to p17 is saturable with a calculated KD of 42 nM. Since size exclusion chromatography of drug-p17 complexes indicates that the active species is a homodimer with a mass of 30-40 kDa, the stoichiometry calculated for the drug-protein complex is approximately 1:1. Furthermore, unlike FKBP-12, chicken p17 bound to FK506 does not bind to calcineurin-calmodulin complexes. This work demonstrates the excision of a domain from an hsp56 protein that is active in binding FK506 and functionally distinct from FKBP-12, a protein of similar size and structure.

show abstract

mentioning

confidence: 55%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

An active FK506-binding domain of 17,000 daltons is isolated following limited proteolysis of chicken thymus HSP56

Yem¹,

Reardon²,

Leone³

et al. 1993

Biochemistry

View full text Add to dashboard Cite

show abstract

“…Like most FKBPs, the protein had a migration rate on SDS−PAGE gel indicative of a higher molecular weight (56−59 kDa) than actually calculated from its sequence (51.8 kDa); hence the confusion in nomenclature. It was subsequently found that FKBP52 was identical to a previously described heat-shock protein (hsp 56) found as a component of several unliganded steroid receptor complexes. ,, FKBP52 contains two FKBP domains with detectable rotamase activity and a third domain which contains three tetratricopeptide repeat motifs . Following these three domains is a calmodulin-binding consensus sequence.…”

Section: The Peptidylprolyl Isomerasesmentioning

confidence: 79%

“…It was subsequently found that FKBP52 was identical to a previously described heat-shock protein (hsp 56) found as a component of several unliganded steroid receptor complexes. 22,23,67 FKBP52 contains two FKBP domains with detectable rotamase activity and a third domain which contains three tetratricopeptide repeat motifs. 68 Following these three domains is a calmodulin-binding consensus sequence.…”

Section: Introductionmentioning

confidence: 99%