Abstract
HslVU, a two-component proteasome-related prokaryotic system is composed of HslV protease and HslU ATPase. HslV protomers assemble in a dodecamer of two-stacked hexameric rings that form a complex with HslU hexamers. The intra- and inter-ring protomer interfaces in the HslV dodecamer underpin the integrity and functionality of HslVU. Structural characterization of HslV from different bacteria illustrated considerable differences in interacting residues, accessible surface and gap volumes at the intra-ring interface that is primarily stabilized by polar interactions. Amino acid residues Lys28, Arg83 and Asp111 have envisaged as hot spots at this HslU-interacting interface. The inter-ring interfaces that are made up of side chain packing of hydrophobic residues are structurally conserved. Hyperthermostable bacterium T. maritima HslV has extensively networked polar/nonpolar interactions and highly packed environment at all interfaces. Present data demonstrates that HslV protomer interfaces perform distinct functions; whereas intra-ring interface participates in HslV:HslU interaction resulting in allosteric activation of HslV protease by HslU, the inter-ring interfaces uphold the oligomeric form of HslV.
Similar content being viewed by others
Abbreviations
- EcV:
-
HslV protease from E. coli
- HiV:
-
HslV protease from H. influenzae
- TmV:
-
HslV protease from T. maritima
- HslVU:
-
two component protease-chaperone complexes
- HslU:
-
HslU chaperone component of HslUV
- Lon:
-
energy-dependent prokaryotic intracellular serine protease
- ClpAP/XP:
-
two component protease-chaperone complexes containing caseinolytic protease ClpP and chaperone ClpA or ClpX
- CD:
-
Circular dichorism
- iASA:
-
interface accessible surface area
References
Azim M. K., Goehring W., Song H. K., Ramachandran R., Bochtler M., Goettig P. (2005) Protein Sci. 14: 1357–1362
Bahadur R. P., Chakarbarti P., Rodier F., Janin J. (2004) J. Mol. Biol. 336: 943–955
Baumeister W., Walz J., Zuhl F., Seemuller E. (1998) Cell 92: 367–380
Bochtler M., Ditzel L., Groll M., Huber R. (1997) Proc. Natl. Acad. Sci. USA 94: 6070–6074
Bochtler M., Hartmann C., Song H. K., Bourenkov G. P., Bartunik H. D., Huber R. (2000) Nature 403: 800–805
DeLano W. (2002) Curr. Opin. Struct. Biol. 12: 14–20
Gabdoulline R. R., Wade R. C., Walter D. (2003) Nucleic Acids Res 31: 3349–3351
Groll M., Clausen T. (2003) Curr. Opin. Struct. Biol. 13: 665–673
Groll M., Bochtler M., Brandstetter H., Clausen T., Huber R. (2005) ChemBioChem 6: 222–256
Keskin O., Ma B., Nussinov R. (2005) J. Mol. Biol. 345: 1281–1294
Kortemme T., Baker D. (2002) Proc. Natl. Acad. Sci. USA 99: 14116–14121
Kortemme, T., Kim, D. E., and Baker, D. (2004) Sci STKE pl2
Laskowski R. A. (1995) J. Mol. Graph 13: 323–330
Li X., Keskin O., Ma B., Nussinov R., Liang J. (2004) J. Mol. Biol. 344: 781–795
Ma B., Elkayam T., Wolfson H., Nussinov R. (2003) Proc. Natl. Acad. Sci. USA 100: 5772–5777
Missiakas D., Schwager F., Betton J. M., Georgopoulos C., Raina S. (1996) EMBO J 15: 6899–6909
Ramachandran R., Hartmann C., Song H. K., Huber R., Bochtler M. (2002) Proc. Natl. Acad. Sci. USA 99: 7396–7401
Reichmann D., Rahat O., Albeck S., Meged R., Dym O., Schreiber G. (2005) Proc. Natl. Acad. Sci. USA 102: 57–62
Rohrwild M., Coux O., Huang H-C., Moerschell R. P., Yoo S. J., Seol J. H., Chung C. H., Goldberg A. L. (1996) Proc. Natl. Acad. Sci. USA 93: 5808–5813
Seong I. S., Kang M. S., Choi M. K., Lee J. W., Koh O. J., Wang J., Eom S. H., Chung C. H. (2002) J. Biol. Chem. 277: 25976–25982
Song H. K., Bochtler M., Azim M. K., Hartmann C., Huber R., Ramachandran R. (2003) Biophys. Chem. 100: 437–452
Sousa M. C., Trame C. B., Tsuruta H., Wilbanks S. M., Reddy V. S., McKay D. B. (2000) Cell 103: 633–643
Wallace A. C., Laskowski R. A., Thornton J. M. (1995) Prot. Eng. 8: 127–134
Won A-R, Kessler B. M., Overkleeft H. S., McKay D. B. (2003) J. Mol. Biol. 330: 185–195
Acknowledgement
We thank Asmat Salim, ICCS, University of Karachi, Karachi, Pakistan for helpful discussion and Elizabeth Weyher, Max Planck Institute for Biochemistry, Germany for CD spectral analysis of HslV.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Azim, M.K., Noor, S. Characterization of Protomer Interfaces in HslV Protease; the Bacterial Homologue of 20S Proteasome. Protein J 26, 213–219 (2007). https://doi.org/10.1007/s10930-006-9048-x
Published:
Issue Date:
DOI: https://doi.org/10.1007/s10930-006-9048-x