The RNA polymerase subunit RPB10 displays a high level of conservation across archaea and eukarya and is required for cell viability in yeast (1, 2). It is a zinc-binding protein (3) 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 (4-6). Binding of RPB10 to this a2-like heterodimer through zinc-mediated hemi-coordination (4) 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 (7). It also interacts with RPB1-3 and 5, and strongly with RPB3.
Recombinant RPB10 is isolated from an E. coli strain that carries the coding sequence of human RPB10 under the control of a T7 promoter. hRPB10 has been applied in protein-protein interactions assays. Protein is greater than 95% homogeneous based on SDS-PAGE analysis. 1 unit equals 1 nanogram of purified protein. 100 units (ng) are sufficient for a protein-protein interaction assay. variable in different lots 1x dilution buffer A: 20 mM Tris-Cl (pH 8.0), 20% Glycerol, 100 mM KCl, 1 mM DTT and 0.2 mM EDTA
References: 1. Mackereth, C.D., et al. (2000), Proc. Natl. Acad. Sci. USA 97, 6316-6321 2. Woychik, R. A., et al., (1990) TIBS 15, 347-351 3. Woychik, N.A., et al., (1990) Genes Dev. 4, 313-323 4. Lalo, D., et al., (1993) Proc. Natl. Acad. Sci. USA 90, 5524-5528 5. Kimura, M., et al., (1997) J. Biol. Chem. 272, 25851-25855 6. Eloranta, J.J., et al., (1998) Nucleic Acids Res. 26, 5562-5567 7. Ishihama, A. (1981) Adv. Biophys. 14, 1-35
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