Chaperone-like activity of the AAA+ proteins Rvb1 and Rvb2 in the assembly of various complexes

Philos Trans R Soc Lond B Biol Sci. 2013 Mar 25;368(1617):20110399. doi: 10.1098/rstb.2011.0399. Print 2013 May 5.


Rvb1 and Rvb2 are highly conserved and essential eukaryotic AAA+ proteins linked to a wide range of cellular processes. AAA+ proteins are ATPases associated with diverse cellular activities and are characterized by the presence of one or more AAA+ domains. These domains have the canonical Walker A and Walker B nucleotide binding and hydrolysis motifs. Rvb1 and Rvb2 have been found to be part of critical cellular complexes: the histone acetyltransferase Tip60 complex, chromatin remodelling complexes Ino80 and SWR-C, and the telomerase complex. In addition, Rvb1 and Rvb2 are components of the R2TP complex that was identified by our group and was determined to be involved in the maturation of box C/D small nucleolar ribonucleoprotein (snoRNP) complexes. Furthermore, the Rvbs have been associated with mitotic spindle assembly, as well as phosphatidylinositol 3-kinase-related protein kinase (PIKK) signalling. This review sheds light on the potential role of the Rvbs as chaperones in the assembly and remodelling of these critical complexes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • ATPases Associated with Diverse Cellular Activities
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • DNA Helicases / genetics
  • DNA Helicases / metabolism*
  • Gene Expression Regulation / physiology
  • Humans
  • Models, Molecular
  • Molecular Chaperones
  • Protein Conformation


  • Carrier Proteins
  • Molecular Chaperones
  • ATPases Associated with Diverse Cellular Activities
  • DNA Helicases
  • RUVBL1 protein, human
  • RUVBL2 protein, human