Literature DB >> 9563823

Sequence motifs shared between chaperone components participating in the assembly of progesterone receptor complexes.

D F Smith1.   

Abstract

Steroid receptors typically exist in a heteromeric complex with Hsp90 and other components of the molecular chaperone machinery. Assembly of functional receptor complexes follows an ordered pathway involving at least eight chaperone components, some only participating in early assembly stages that are prerequisite for formation of mature complexes. The mechanisms directing the order of assembly steps and the nature of transitional interactions between assembly steps are largely unknown, but likely are encoded in the primary sequence and functional domains of the participating chaperones. Several common sequence motifs are shared between participants that may be key in ordering the steroid receptor assembly pathway.

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Year:  1998        PMID: 9563823     DOI: 10.1515/bchm.1998.379.3.283

Source DB:  PubMed          Journal:  Biol Chem        ISSN: 1431-6730            Impact factor:   3.915


  10 in total

1.  Heat shock cognate protein 70 chaperone-binding site in the co-chaperone murine stress-inducible protein 1 maps to within three consecutive tetratricopeptide repeat motifs.

Authors:  J Van Der Spuy; B D Kana; H W Dirr; G L Blatch
Journal:  Biochem J       Date:  2000-02-01       Impact factor: 3.857

2.  Reconstitution of a functional duck hepatitis B virus replication initiation complex from separate reverse transcriptase domains expressed in Escherichia coli.

Authors:  J Beck; M Nassal
Journal:  J Virol       Date:  2001-08       Impact factor: 5.103

3.  Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90.

Authors:  A Chadli; I Bouhouche; W Sullivan; B Stensgard; N McMahon; M G Catelli; D O Toft
Journal:  Proc Natl Acad Sci U S A       Date:  2000-11-07       Impact factor: 11.205

4.  Inhibition of double-stranded RNA- and tumor necrosis factor alpha-mediated apoptosis by tetratricopeptide repeat protein and cochaperone P58(IPK).

Authors:  N M Tang; M J Korth; M Gale; M Wambach; S D Der; S K Bandyopadhyay; B R Williams; M G Katze
Journal:  Mol Cell Biol       Date:  1999-07       Impact factor: 4.272

5.  Geldanamycin selectively targets the nascent form of ERBB3 for degradation.

Authors:  Candice S Gerbin; Ralf Landgraf
Journal:  Cell Stress Chaperones       Date:  2010-01-19       Impact factor: 3.667

6.  Interference between proteins Hap46 and Hop/p60, which bind to different domains of the molecular chaperone hsp70/hsc70.

Authors:  M Gebauer; M Zeiner; U Gehring
Journal:  Mol Cell Biol       Date:  1998-11       Impact factor: 4.272

7.  Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast.

Authors:  Robert T Youker; Peter Walsh; Traude Beilharz; Trevor Lithgow; Jeffrey L Brodsky
Journal:  Mol Biol Cell       Date:  2004-09-01       Impact factor: 4.138

8.  Duplicate gene evolution toward multiple fates at the Drosophila melanogaster HIP/HIP-Replacement locus.

Authors:  Catherine C Hogan; Brian R Bettencourt
Journal:  J Mol Evol       Date:  2009-03-31       Impact factor: 2.395

9.  Comparison of the carboxy-terminal DP-repeat region in the co-chaperones Hop and Hip.

Authors:  Gregory M Nelson; Holly Huffman; David F Smith
Journal:  Cell Stress Chaperones       Date:  2003       Impact factor: 3.667

10.  In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis.

Authors:  W M Obermann; H Sondermann; A A Russo; N P Pavletich; F U Hartl
Journal:  J Cell Biol       Date:  1998-11-16       Impact factor: 10.539

  10 in total

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