RVB2 cDNA ORF clone, Saccharomyces cerevisiae S288C

The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.
Bussey H, Storms RK, Ahmed A, Albermann K, Allen E, Ansorge W, Araujo R, Aparicio A, Barrell B, Badcock K, Benes V, Botstein D, Bowman S, Br?ckner M, Carpenter J, Cherry JM, Chung E, Churcher C, Coster F, Davis K, Davis RW, Dietrich FS, Delius H, DiPaolo T, Hani J
Nature387(6632 Suppl)103-5(1997 May)

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

Data show that the 14 different polypeptide containing chromatin-remodeling complex SWR1 contains a single heterohexameric Rvb1/Rvb2 ring that, together with the catalytic subunit Swr1, brackets two independently assembled multisubunit modules.
Title: Molecular architecture of the ATP-dependent chromatin-remodeling complex SWR1.

Existence of a novel role for Tel2, namely in transcription, possibly in cooperation with Rvb2 and involving the existence of physical interactions with the Med15/Gal11 Mediator subunit.
Title: Genetic and physical interactions between Tel2 and the Med15 Mediator subunit in Saccharomyces cerevisiae.

purified endogenous untagged Rvb1/Rvb2 complexes were found as single hexameric rings, similar to the complexes assembled in vitro from purified untagged components
Title: Alternative oligomeric states of the yeast Rvb1/Rvb2 complex induced by histidine tags.

Rvb2p, cooperatively binds single-stranded DNA as monomers. Binding stimulates a slow ATPase activity and supports a 3'- to 5' DNA unwinding activity that requires a 3'-protruding tail >or= 30 nucleotides.
Title: 3'- to 5' DNA unwinding by TIP49b proteins.

Pontin and reptin could acquire distinct structural states to regulate their broad functions as molecular motors and scaffolds for nucleic acids and proteins.
Title: Architecture of the pontin/reptin complex, essential in the assembly of several macromolecular complexes.