Nucleotide-dependent Oligomerization of ClpB from Escherichia Coli

Overview

Journal Protein Sci

Specialty Biochemistry

Date 1999 Sep 24

PMID 10493591

Citations 28

Authors

M Zolkiewski

M Kessel

A Ginsburg

M R Maurizi

Affiliations

Soon will be listed here.

Abstract

Self-association of ClpB (a mixture of 95- and 80-kDa subunits) has been studied with gel filtration chromatography, analytical ultracentrifugation, and electron microscopy. Monomeric ClpB predominates at low protein concentration (0.07 mg/mL), while an oligomeric form is highly populated at >4 mg/mL. The oligomer formation is enhanced in the presence of 2 mM ATP or adenosine 5'-O-thiotriphosphate (ATPgammaS). In contrast, 2 mM ADP inhibits full oligomerization of ClpB. The apparent size of the ATP- or ATPgammaS-induced oligomer, as determined by gel filtration, sedimentation velocity and electron microscopy image averaging, and the molecular weight, as determined by sedimentation equilibrium, are consistent with those of a ClpB hexamer. These results indicate that the oligomerization reactions of ClpB are similar to those of other Hsp100 proteins.

Citing Articles

Hsp100 Molecular Chaperone ClpB and Its Role in Virulence of Bacterial Pathogens.

Kedzierska-Mieszkowska S, Zolkiewski M Int J Mol Sci. 2021; 22(10).

PMID: 34070174 PMC: 8158500. DOI: 10.3390/ijms22105319.

AAA+ Molecular Chaperone ClpB in : Its Role and Significance in Leptospiral Virulence and Pathogenesis of Leptospirosis.

Kedzierska-Mieszkowska S, Arent Z Int J Mol Sci. 2020; 21(18).

PMID: 32932775 PMC: 7555560. DOI: 10.3390/ijms21186645.

Significance of Individual Domains of ClpL: A Novel Chaperone from .

Jana B, Biswas I Biochemistry. 2020; 59(36):3368-3379.

PMID: 32791831 PMC: 7875316. DOI: 10.1021/acs.biochem.0c00544.

Interaction of substrate-mimicking peptides with the AAA+ ATPase ClpB from Escherichia coli.

Ranaweera C, Glaza P, Yang T, Zolkiewski M Arch Biochem Biophys. 2018; 655:12-17.

PMID: 30092228 PMC: 6139261. DOI: 10.1016/j.abb.2018.08.002.

The Chaperonin GroEL: A Versatile Tool for Applied Biotechnology Platforms.

ONeil P, Machen A, Deatherage B, Trecazzi C, Tischer A, Machha V Front Mol Biosci. 2018; 5:46.

PMID: 29868607 PMC: 5962814. DOI: 10.3389/fmolb.2018.00046.

References

Zamyatnin A . Amino acid, peptide, and protein volume in solution. Annu Rev Biophys Bioeng. 1984; 13:145-65. DOI: 10.1146/annurev.bb.13.060184.001045. View

Glover J, Lindquist S . Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell. 1998; 94(1):73-82. DOI: 10.1016/s0092-8674(00)81223-4. View

Squires C, Pedersen S, Ross B, Squires C . ClpB is the Escherichia coli heat shock protein F84.1. J Bacteriol. 1991; 173(14):4254-62. PMC: 208084. DOI: 10.1128/jb.173.14.4254-4262.1991. View

Parsell D, Sanchez Y, Stitzel J, Lindquist S . Hsp104 is a highly conserved protein with two essential nucleotide-binding sites. Nature. 1991; 353(6341):270-3. DOI: 10.1038/353270a0. View

Woo K, Kim K, GOLDBERG A, Ha D, Chung C . The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase. J Biol Chem. 1992; 267(28):20429-34. View

Stafford 3rd W . Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal Biochem. 1992; 203(2):295-301. DOI: 10.1016/0003-2697(92)90316-y. View

Park S, Kim K, Woo K, Seol J, Tanaka K, Ichihara A . Site-directed mutagenesis of the dual translational initiation sites of the clpB gene of Escherichia coli and characterization of its gene products. J Biol Chem. 1993; 268(27):20170-4. View

Parsell D, Kowal A, Lindquist S . Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes. J Biol Chem. 1994; 269(6):4480-7. View

Parsell D, Kowal A, Singer M, Lindquist S . Protein disaggregation mediated by heat-shock protein Hsp104. Nature. 1994; 372(6505):475-8. DOI: 10.1038/372475a0. View

10.

SHAPIRO B, Ginsburg A . Effects of specific divalent cations on some physical and chemical properties of glutamine synthetase from Escherichia coli. Taut and relaxed enzyme forms. Biochemistry. 1968; 7(6):2153-67. DOI: 10.1021/bi00846a018. View

11.

Hess H, Derr J . Assay of inorganic and organic phosphorus in the 0.1-5 nanomole range. Anal Biochem. 1975; 63(2):607-13. DOI: 10.1016/0003-2697(75)90388-7. View

12.

Lanzetta P, Alvarez L, Reinach P, Candia O . An improved assay for nanomole amounts of inorganic phosphate. Anal Biochem. 1979; 100(1):95-7. DOI: 10.1016/0003-2697(79)90115-5. View

13.

Kim K, Woo K, Seong I, LEE Z, Baek S, Chung C . Mutational analysis of the two ATP-binding sites in ClpB, a heat shock protein with protein-activated ATPase activity in Escherichia coli. Biochem J. 1998; 333 ( Pt 3):671-6. PMC: 1219631. DOI: 10.1042/bj3330671. View

14.

Wickner S, Gottesman S, Skowyra D, Hoskins J, McKenney K, Maurizi M . A molecular chaperone, ClpA, functions like DnaK and DnaJ. Proc Natl Acad Sci U S A. 1994; 91(25):12218-22. PMC: 45408. DOI: 10.1073/pnas.91.25.12218. View

15.

Maurizi M, Thompson M, Singh S, Kim S . Endopeptidase Clp: ATP-dependent Clp protease from Escherichia coli. Methods Enzymol. 1994; 244:314-31. DOI: 10.1016/0076-6879(94)44025-5. View

16.

Wawrzynow A, Wojtkowiak D, Marszalek J, Banecki B, Jonsen M, Graves B . The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone. EMBO J. 1995; 14(9):1867-77. PMC: 398286. DOI: 10.1002/j.1460-2075.1995.tb07179.x. View

17.

Kessel M, Maurizi M, Kim B, Kocsis E, Trus B, Singh S . Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome. J Mol Biol. 1995; 250(5):587-94. DOI: 10.1006/jmbi.1995.0400. View

18.

Pace C, Vajdos F, Fee L, Grimsley G, Gray T . How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 1995; 4(11):2411-23. PMC: 2143013. DOI: 10.1002/pro.5560041120. View

19.

Schirmer E, Glover J, Singer M, Lindquist S . HSP100/Clp proteins: a common mechanism explains diverse functions. Trends Biochem Sci. 1996; 21(8):289-96. View

20.

Kessel M, Wu W, Gottesman S, Kocsis E, Steven A, Maurizi M . Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY. FEBS Lett. 1996; 398(2-3):274-8. DOI: 10.1016/s0014-5793(96)01261-6. View