Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Cell Mol Life Sci. 2013 Mar;70(5):761-75. doi: 10.1007/s00018-012-1076-4. Epub 2012 Jul 18.

Architecture and regulation of HtrA-family proteins involved in protein quality control and stress response.

Author information

  • 1Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, 23538, Lübeck, Germany. hansen@biochem.uni-luebeck.de

Abstract

Protein quality control is vital for all living cells and sophisticated molecular mechanisms have evolved to prevent the excessive accumulation of unfolded proteins. High-temperature requirement A (HtrA) proteases have been identified as important ATP-independent quality-control factors in most species. HtrA proteins harbor a serine-protease domain and at least one peptide-binding PDZ domain to ensure efficient removal of misfolded or damaged proteins. One distinctive property of HtrAs is their ability to assemble into complex oligomers. Whereas all examined HtrAs are capable of forming pyramidal 3-mers, higher-order complexes consisting of up to 24 molecules have been reported. Tight control of chaperone and protease function is of pivotal importance in preventing deleterious HtrA-protease activity. In recent years, structural biology provided detailed insights into the molecular basis of the regulatory mechanisms, which include unique intramolecular allosteric signaling cascades and the dynamic switching of oligomeric states of HtrA proteins. Based on these results, functional models for many family members have been developed. The HtrA protein family represents a remarkable example of how structural and functional diversity is attained from the assembly of simple molecular building blocks.

PMID:
22806565
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for Springer
    Loading ...
    Write to the Help Desk