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RPC19 Rpc19p

AC19, RPC19, RPA17
The protein encoded by this gene is a component of the RNA polymerase I and RNA polymerase III complexes, which function in the synthesis of ribosomal RNA precursors and small RNAs, respectively. Mutations in this gene are a cause of Treacher Collins syndrome (TCS), a craniofacial development disorder. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2011] (from NCBI)
Top mentioned proteins: POLYMERASE, AC40, ACID, CAN, fibrillin-1
Papers on AC19
Subunit compositions of Arabidopsis RNA polymerases I and III reveal Pol I- and Pol III-specific forms of the AC40 subunit and alternative forms of the C53 subunit.
Pikaard et al., Saint Louis, United States. In Nucleic Acids Res, May 2015
In all eukaryotes examined to date, AC40 and AC19 subunits are common to Pol I (a.k.a.
Rbs1, a new protein implicated in RNA polymerase III biogenesis in yeast Saccharomyces cerevisiae.
Boguta et al., Warsaw, Poland. In Mol Cell Biol, Apr 2015
Rbs1 physically interacts with a subset of Pol III subunits, AC19, AC40, and ABC27/Rpb5.
Mutations in genes encoding subunits of RNA polymerases I and III cause Treacher Collins syndrome.
Wieczorek et al., Leiden, Netherlands. In Nat Genet, 2011
heterozygous mutations of POLR1D in 252 individuals with Treacher Collins syndrome
Characterization of the RNA polymerase II and III complexes in Leishmania major.
Myler et al., Seattle, United States. In Int J Parasitol, 2007
The latter experiments also identified the RNAP III subunits RPC1 (C160), RPC2 (C128), RPC3 (C82), RPC4 (C53), RPC5 (C37), RPC6 (C34), RPC9 (C17), RPAC1 (AC40) and RPAC2 (AC19).
Purification of an eight subunit RNA polymerase I complex in Trypanosoma brucei.
Günzl et al., Farmington, United States. In Mol Biochem Parasitol, 2006
In addition to the already known subunits RPA1, RPA2, RPC40, 1RPB5, and RPA12, the complex contained RPC19, RPB8, and 1RPB10.
A kinetic framework for a mammalian RNA polymerase in vivo.
Misteli et al., Bethesda, United States. In Science, 2002
analyzed the kinetics of assembly and elongation of the RNA polymerase I complex on endogenous ribosomal genes in the nuclei of living cells with the use of in vivo microscopy
Isolation and characterization of the fission yeast gene rpa42+, which encodes a subunit shared by RNA polymerases I and III.
Nogi et al., Saitama, Japan. In Mol Gen Genet, 1999
To gain insight into the functions of alpha-related subunits in eukaryotes, we have previously identified the alpha-related small subunit RPA17 of RNA polymerase I (and III) in Schizosaccharomyces pombe, and have shown that it is a functional homolog of Saccharomyces cerevisiae AC19.
Rpc19 and Rpc40, two alpha-like subunits shared by nuclear RNA polymerases I and III, are interchangeable between the fission and budding yeasts.
Shematorova et al., Moscow, Russia. In Curr Genet, 1999
The cDNAs and genes encoding the common subunits Rpc19 and Rpc40 of nuclear RNA polymerases I and III of Schizosaccharomyces pombe were isolated from cDNA and genomic libraries of the fission yeast and tested for their ability to substitute for the homologous genes in Saccharomyces cerevisiae by heterospecific complementation of corresponding null alleles and temperature-sensitive mutations.
A protein-protein interaction map of yeast RNA polymerase III.
Werner et al., Gif-sur-Yvette, France. In Proc Natl Acad Sci U S A, 1999
Four subunits that are common to pol I, II, and III (ABC27, ABC14.5, ABC10alpha, and ABC10beta), two that are common to pol I and III (AC40 and AC19), and one pol III-specific subunit (C11) can associate with defined regions of the two large subunits.
FRAXAC1 and DXS548 polymorphisms in the Chinese population.
Brown et al., Hong Kong, Hong Kong. In Am J Med Genet, 1999
There are more AC18 repeat alleles and fewer AC19 repeat alleles.
The fission yeast rpa17+ gene encodes a functional homolog of AC19, a subunit of RNA polymerases I and III of Saccharomyces cerevisiae.
Nogi et al., Saitama, Japan. In Mol Gen Genet, 1999
RPA17 has 125 amino acids and shows 63% identity to AC19 over a 108-residue stretch, whereas the N-terminal regions of the two proteins are highly divergent.
In vitro assembly of an archaeal D-L-N RNA polymerase subunit complex reveals a eukaryote-like structural arrangement.
Weinzierl et al., London, United Kingdom. In Nucleic Acids Res, 1999
D also interacts under the same conditions with the RPB11 and AC19 subunits from the yeast Saccharomyces cerevisiae, suggesting that essential elements of the binding surface between these proteins have been conserved across the archaeal/eukaryotic evolutionary domain boundary.
The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces cerevisiae reveals an unusually high number of overlapping open reading frames.
Valle et al., Padova, Italy. In Yeast, 1997
Similarity searches against DNA and protein data banks show that six ORFs correspond to already known yeast genes (OMP1, PSU1, MLS1, RPC19, DBP2, CYB5) and one ORF matches the sequence of a putative yeast gene (ESBP6).
Mouse RNA polymerase I 16-kDa subunit able to associate with 40-kDa subunit is a homolog of yeast AC19 subunit of RNA polymerases I and III.
Muramatsu et al., Morohongō, Japan. In J Biol Chem, 1997
Characterization of the homologous mouse protein.
Localization of yeast RNA polymerase I core subunits by immunoelectron microscopy.
Schultz et al., Illkirch-Graffenstaden, France. In Embo J, 1996
Polyclonal antibodies outlined the alpha-like subunit AC40 and subunit AC19 which were found co-localized also in the apical region of the enzyme.
Association between 36- and 13.6-kDa alpha-like subunits of Arabidopsis thaliana RNA polymerase II.
Guilfoyle et al., Columbia, United States. In J Biol Chem, 1996
AC40 and AC19 in yeast) contain one or two motifs related to the alpha subunit in prokaryotic RNA polymerases.
Interactions between three common subunits of yeast RNA polymerases I and III.
Thuriaux et al., Gif-sur-Yvette, France. In Proc Natl Acad Sci U S A, 1993
The AC40 and AC19 subunits (encoded by RPC40 and RPC19) are shared by yeast RNA polymerases I and III and have a local sequence similarity to prokaryotic alpha subunits.
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