Identification and characterization of a Hsp70 (DnaK) chaperone system from Meiothermus ruber

Molecular Genetics and Genomics

Volumn 269, Issue 1, 2003, Pages 109-115

  Pleckaityte, M ^a   Mistiniene, E ^a   Michailoviene, V ^a   Zvirblis, G ^a  

^a VILNIUS UNIVERSITY   (Lithuania)

Author keywords

Chaperone; Chaperone activity; Cross linking; Meiothermus ruber; Size exclusion chromatography

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; CHAPERONE; CYSTEINE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 22; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; MALATE DEHYDROGENASE; MITOCHONDRIAL ENZYME; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENE; CONTROLLED STUDY; ENZYME DENATURATION; GEL PERMEATION CHROMATOGRAPHY; GENE FUNCTION; GENE IDENTIFICATION; GENE STRUCTURE; GENETIC ANALYSIS; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; OPERON; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FOLDING; SEQUENCE HOMOLOGY; THERMOPHILIC BACTERIUM; THERMUS THERMOPHILUS;

BACTERIA (MICROORGANISMS); MEIOTHERMUS RUBER; THERMUS THERMOPHILUS;

EID: 0038216546     PISSN: 16174615     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00438-003-0818-2     Document Type: Article

References (25)

1. Banecki B, Liberek K, Wall D, Wawrzynow A, Georgopoulos C, Bertoli E, Tanfani F, Zylicz M (1996) Structure-function analysis of the zinc finger region of the DnaJ molecule chaperone. J Biol Chem 271:14840-4848
2. Bukau B, Horwich AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92:351-366
3. Cunningham BC, Mulkerrin MG, Wells JA (1991) Dimerization of human growth hormone by zinc, Science 253:545-548
4. Diamant S, Ben-Zvi AP, Bukau B, Goloubinoff P (2000) Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. J Biol Chem 520:25-29
5. Dienys G, Sereikaite J, Gavenas G, Kvederas R, Bumelis VA (1998) Cross-linking of protein subunits by 1,3,5-triacryloyl-hexahydro-S-triazine. Bioconjugate Chem 9:744-748
6. Dienys G, Sereikaite J, Luksa V, Jarutiene O, Mistiniene E, Bumelis VA (2000) Dimerization of human growth hormone in the presence of metal ions. Bioconjugate Chem 11:646-651
7. Ferreira AM, Wait R, Nobre MF, da Costa MS (1999) Characterization of glycolipids from Meiothermus spp. Microbiology 145:1191-1199
8. Goloubinoff P, Mogk A, Ben Zvi AP, Tomoyasu T, Bukau B (1999) Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci USA 96:13732-13737
9. Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381:571-580
10. Hartl FU, Hayer-Hartl M (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 296:1852-1858
11. Herbort M, Schon U, Angermann K, Lang J, Schumann W (1996) Cloning and sequencing of the dnaK operon of Bacillus stearothermophilus. Gene 170:81-84
12. Laufen T, Mayer MP, Beisel C, Klostermeier D, Mogk A, Reinstein J, Bukau B (1999) Mechanism of regulation of Hsp40 chaperones by DnaJ cochaperone. Proc Natl Acad Sci USA 96:5452-5457
13. Loginova LG, Bogdanova TI (1991) Bacteria of gender Thermus and their thermostable enzymes. Biotechnologija (Moskva) 3:23-27
14. Martinez-Yamout M, Legge GB, Zhang O, Wright PE, Dyson HJ (2000) Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ. J Mol Biol 300:805-818
15. Motohashi K, Taguchi H, Ishii N, Yoshida M (1994) Isolation of the stable hexameric DnaK-DnaJ complex from Thermus thermophilus. J Biol Chem 269:27074-27079
16. Motohashi K, Yohda M, Endo I, Yoshida M (1996) A novel factor required for the assembly of the DnaK and DnaJ chaperones of Thermus thermophilus. J Biol Chem 271:17343-17348
17. Rüdiger S, Schneider-Mergener J, Bukau B (2001) Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. EMBO J 20:1042-1050
18. Nobre MF, Truper HG, da Costa MS (1996) Transfer of Thermus ruber (Loginova et al. 1984), Thermus silvanus (Tenreiro et al. 1995) and Thermus chliarophilus (Tenreiro et al. 1995) to Meiothermus gen. nov. as Meiothermus ruber comb. nov., Meiothermus silvanus comb. nov. and Meiothermus chliarophilus comb. nov., respertively, and emendation of the genus Thermus. Int J Syst Bacteriol 46:604-606
19. Sambrook J, Fritsch EF, Maniatis T (1989) Molecular cloning: a laboratory manual, (2nd edn). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
20. Sanchez SA, Hazlett TL, Brunet JU, Jameson DM (1998) Aggregation states of mitochondrial malate dehydrogenase. Protein Sci 7:2184-2189
21. Sha B, Lee S, Cyr DM (2000) The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1. Structure 15 799-807
22. Suh WC, Burkholder WF, Lu CZ, Zhao X, Gottesman ME, Gross CA (1998) Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ. Proc Natl Acad Sci USA 95:15223-15228
23. Szabo A, Korszun R, Hartl FU, Flanagan J (1996) A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. EMBO J 15:408-417
24. Thulasiraman V, Yang CF, Frydman J (1999) In vivo newly translated polypeptides are sequestered in a protected folding environment. EMBO J 18:85-95
25. Wawrzynow A, Zylicz M (1995) Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates. J Biol Chem 270:19300-19306