Small glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activity

Cell Stress and Chaperones

Volumn 7, Issue 3, 2002, Pages 258-268

  Angeletti, Peter C ^a   Walker, Doriann ^b   Panganiban, Antonito T ^a,b  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b UNIVERSITY OF NEW MEXICO SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; LUCIFERASE; SMALL GLUTAMINE RICH PROTEIN; U BINDING PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; ASSAY; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME REGULATION; FUNGAL STRAIN; GENE ACTIVITY; HUMAN; HUMAN CELL; IN VITRO STUDY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; SEQUENCE HOMOLOGY; WILD TYPE;

ADENOSINE TRIPHOSPHATASES; CARRIER PROTEINS; DNA REPLICATION; GENE DELETION; GLUTAMINE; HELA CELLS; HIV; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; MOLECULAR CHAPERONES; MUTAGENESIS; PARVOVIRUS; PROTEIN FOLDING; PROTEINS; VIRION; VIRUS REPLICATION;

HUMULUS;

EID: 0036665912     PISSN: 13558145     EISSN: None     Source Type: Journal    
DOI: 10.1379/1466-1268(2002)007<0258:SGRPVP>2.0.CO;2     Document Type: Article

References (36)

1. Angeletti PC, Engler JA. 1996. Tyrosine kinase-dependent release of an adenovirus preterminal protein complex from the nuclear matrix. J Virol 70: 3060-3067.
2. Angeletti PC, Engler JA. 1998. Adenovirus preterminal protein binds to the CAD enzyme at active sites of viral DNA replication on the nuclear matrix. J Virol 72: 2896-2904.
3. Ballinger CA, Connell P, Wu Y, Hu Z, Thompson LJ, Yin LY, Patterson C. 1999. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol Cell Biol 19: 4535-4545.
4. Bimston D, Song J, Winchester D, Takayama S, Reed JC, Morimoto RI. 1998. BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release. EMBO J 17: 6871-6878.
5. Callahan MA, Handley MA, Lee YH, Talbot KJ, Harper JW, Panganiban AT. 1998. Functional interaction of human immunodeficiency virus type 1 Vpu and Gag with a novel member of the tetratricopeptide repeat protein family [published erratum appears in J Virol 1998 72: 8461]. J Virol 72: 5189-5197.
6. Chen S, Smith DF. 1998. Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery. J Biol Chem 273: 35194-35200.
7. Connell P, Ballinger CA, Jiang J, Wu Y, Thompson LJ, Hohfeld J, Patterson C. 2001. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat Cell Biol 3: 93-96.
8. Cziepluch C, Kordes E, Poirey R, Grewenig A, Rommelaere J, Jauniaux JC. 1998. Identification of a novel cellular TPR-containing protein, SGT, that interacts with the nonstructural protein NS1 of parvovirus H-1. J Virol 72: 4149-4156.
9. Cziepluch C, Lampel S, Grewenig A, Grund C, Lichter P, Rommelaere J. 2000. H-1 parvovirus-associated replication bodies: a distinct virus-induced nuclear structure. J Virol 74: 4807-4815.
10. Das AK, Cohen PW, Barford D. 1998. The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J 17: 1192- 1199.
11. Frydman J. 2001. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu Rev Biochem 70: 603-647.
12. Ha JH, McKay DB. 1995. Kinetics of nucleotide-induced changes in the tryptophan fluorescence of the molecular chaperone Hsc70 and its subfragments suggest the ATP-induced conformational change follows initial ATP binding. Biochemistry 34: 11635-11644.
13. Hampsey M. 1997. A review of phenotypes in Saccharomyces cerevisiae. Yeast 13: 1099-1133.
14. Hirano T, Kinoshita N, Morikawa K, Yanagida M. 1990. Snap helix with knob and hole: essential repeats in S. pombe nuclear protein nuc2+, Cell 60: 319-328.
15. Hoffmann HJ, Lyman SK, Lu C, Petit MA, Echols H. 1992. Activity of the Hsp70 chaperone complex - DnaK, DnaJ, and GrpE - in initiating phage lambda DNA replication by sequestering and releasing lambda P protein. Proc Natl Acad Sci U S A 89: 12108-12111.
16. Hohfeld J, Minami Y, Hard FU. 1995. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83: 589-598.
17. Irmer H, Hohfeld J. 1997. Characterization of functional domains of the eukaryotic co-chaperone Hip. J Biol Chem 272: 2230-2235.
18. Jiang J, Ballinger CA, Wu Y, Dai Q, Cyr DM, Hohfeld J, Patterson C. 2001. CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. J Biol Chem 13: 13.
19. Johnson BD, Schumacher RJ, Ross ED, Toft DO. 1998. Hop modulates Hsp70/Hsp90 interactions in protein folding. J Biol Chem 273: 3679-3686.
20. Johnson ER, McKay DB. 1999. Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein. Biochemistry 38: 10823-10830.
21. Li H, Soderbarg K, Houshmand H, You ZY, Magnusson G. 2001. Effect on polyomavirus T-antigen function of mutations in a conserved leucine-rich segment of the DnaJ domain. J Virol 75: 2253-2261.
22. Liberek K, Skowyra D, Zylicz M, Johnson C, Georgopoulos C. 1991. The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein. J Biol Chem 266: 14491-14496.
23. Liu FH, Wu SJ, Hu SM, Hsiao CD, Wang C. 1999. Specific interaction of the 70-kDa heat shock cognate protein with the tetratrico-peptide repeats. J Biol Chem 274: 34425-34432.
24. Liu JS, Kuo SR, Makhov AM, Cyr DM, Griffith JD, Broker TR, Chow LT. 1998. Human Hsp70 and Hsp40 chaperone proteins facilitate human papillomavirus-11 E1 protein binding to the origin and stimulate cell-free DNA replication. J Biol Chem 273: 30704-30712.
25. Lu Z, Cyr DM. 1998. Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1. J Biol Chem 273: 27824-27830.
26. Matthews S, Barlow P, Boyd J, et al. 1994. Structural similarity between the p17 matrix protein of HIV-1 and interferon-gamma. Nature 370: 666-668.
27. Meacham GC, Patterson C, Zhang W, Younger JM, Cyr DM. 2001. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat Cell Biol 3: 100-105.
28. Nicolet CM, Craig EA. 1991. Inducing and assaying heat-shock response in Saccharomyces cerevisiae. Methods Enzymol 194: 710- 717.
29. Paillart JC, Gottlinger HG. 1999. Opposing effects of human immunodeficiency virus type 1 matrix mutations support a myristyl switch model of gag membrane targeting. J Virol 73: 2604-2612.
30. Peitzsch RM, McLaughlin S. 1993. Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins. Biochemistry 32: 10436-10443.
31. Ratajczak T, Carrello A. 1996. Cyclophilin 40 (CyP-40), mapping of its hsp90 binding domain and evidence that FKBP52 competes with CyP-40 for hsp90 binding. J Biol Chem 271: 2961-2965.
32. Rothstein R. 1991. Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Methods Enzymol 194: 281-301.
33. Sanchez Y, Lindquist SL. 1990. HSP104 required for induced thermotolerance. Science 248: 1112-1115.
34. Schiestl RH, Manivasakam P, Woods RA, Gietz RD. 1993. Introducing plasmid DNA into yeast by transformation. Methods Companion Methods Enzymol 5: 79-85.
35. Smith DF, Sullivan WP, Marion TN, Zaitsu K, Madden B, McCormick DJ, Toft DO. 1993. Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70. Mol Cell Biol 13: 869-876.
36. Tobaben S, Thakur P, Fernandez-Chacon R, Sudhof TC, Rettig J, Stahl B. 2001. A trimeric protein complex functions as a synaptic chaperone machine. Neuron 31: 987-999.