The RNA polymerase subunit RPB10 displays a high level of conservation across archaea and eukarya and is required for cell viability in yeast. It is a zinc-binding protein with an atypical CX2CXnCC metal binding motif. RPB10 participates in protein-protein interactions with additional components of the polymerase holoenzyme. Experimentally, the binding of RPB10 to an RPB3-RPB11 (or RPAC40-RPAC19 in RNAPI/III) heterodimer is well characterized and persists in both eukaryal and archaeal RNAPs. Binding of RPB10 to this a2-like heterodimer through zinc-mediated hemi-coordination suggests an early role in holoenzyme assembly since the formation of the α2-complex is the first step in the assembly of the prokaryotic RNAPs.
forma física
Clear and colorless frozen liquid solution
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Trends in biochemical sciences, 15(9), 347-351 (1990-09-01)
RNA polymerase II is the core of the complex apparatus that is responsible for the regulated synthesis of mRNA. A comprehensive knowledge of RNA polymerase II is essential to our understanding of the molecular mechanisms through which a variety of
Proceedings of the National Academy of Sciences of the United States of America, 97(12), 6316-6321 (2000-06-07)
The RNA polymerase subunit RPB10 displays a high level of conservation across archaea and eukarya and is required for cell viability in yeast. Structure determination of this RNA polymerase subunit from Methanobacterium thermoautotrophicum reveals a topology, which we term a
RNA polymerases I, II, and III share three subunits that are immunologically and biochemically indistinguishable. The Saccharomyces cerevisiae genes that encode these subunits (RPB5, RPB6, and RPB8) were isolated and sequenced, and their transcriptional start sites were deduced. RPB5 encodes
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