Cloning and identification of the gene coding for the 140-kd subunit of <i>Drosophila</i>
 RNA polymerase II

Faust, Daniela M.; Renkawitz‐Pohl, Renate; Falkenburg, Dieter; Gasch, Alexander; Bialojan, Siegfried; Young, Richard A.; Bautz, Ekkehard K. F.

doi:10.1002/j.1460-2075.1986.tb04276.x

Cited by 15 publications

(4 citation statements)

References 32 publications

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“…Cells containing rpb3-1 on centromerecontaining plasmids grew at wild-type rates at 24°C but arrested growth after three to four divisions at 38°C. Cell viability declined approximately twofold after 16 h at 38°C. Sequence analysis of rpb3-1 DNA revealed two mutations.…”

Section: Mapping Of Rpb3 Physical and Genetic Mapping Revealedmentioning

confidence: 98%

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RNA polymerase II subunit RPB3 is an essential component of the mRNA transcription apparatus.

Kolodziej¹,

Young²

1989

Mol. Cell. Biol.

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To improve our understanding of RNA polymerase H, the gene that encodes its third-largest subunit, RPB3, was isolated from a kgtll DNA library by using antibody probes. The RPB3 DNA sequence predicts a 318-amino-acid protein whose sequence was confirmed, in part, by microsequence analysis of the gel-purified RNA polymerase H subunit. RPB3 was found to be an essential single-copy gene that is tightly linked to HIS6 on chromosome IX. An RPB3 temperature-sensitive mutant that arrested growth after three to four generations at the restrictive temperature was isolated. When the mutant was shifted to the restrictive temperature, RNA polymerase H could no longer assemble, previously assembled functional enzyme was depleted, and mRNA levels were consequently reduced. These results demonstrate that RPB3 is an essential component of the mRNA transcription apparatus. Finally, the RPB3 protein is similar in sequence and length to RPC5, a subunit common to RNA polymerases I and Ill, suggesting that these subunits may play similar roles in RNA polymerases I, II, and HI.Eucaryotic RNA polymerases I, II, and III synthesize large rRNAs, pre-mRNAs, and small rRNAs and tRNAs, respectively (26,35,36). The three RNA polymerases are defined by the components that copurify with transcriptional activity in nonspecific elongation assays. They appear to be composed of 9 to 14 polypeptides whose molecular mass ranges from 10 to 240 kilodaltons (kDa). The subunit architectures and antigenicities of these RNA polymerases are well conserved among eucaryotes. The primary structures, relative stoichiometries, and transcriptional functions of eucaryotic RNA polymerase subunits are ill characterized.The Escherichia coli RNA polymerase has been well defined structurally, and specific functions have been attributed to each of its subunits (reviewed in references 11 and 43). The procaryotic enzyme is composed of four different polypeptides, a (rpoA), 1 (rpoB), 1' (rpoC), and a (rpoD).The sequences of the rpo genes indicate that a, 1, 1', and or are 36,511, 150,543, 155,163 and 70,263 Da,

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Section: Mapping Of Rpb3 Physical and Genetic Mapping Revealedmentioning

confidence: 98%

“…The largest subunits of RNA polymerases I, II, and III are homologs of the procaryotic 1' subunit (1,2,5,31). The second-largest subunit of RNA polymerase II is homologous to 1 (16,38) and is related antigenically to counterparts in RNA polymerases I and III (36). The smaller components of these eucaryotic enzymes remain ill defined.…”

mentioning

confidence: 99%

RNA polymerase II subunit RPB3 is an essential component of the mRNA transcription apparatus.

Kolodziej¹,

Young²

1989

Mol. Cell. Biol.

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“…Whether this compensatory mechanism acts at the transcriptional or translational level is presently under investigation. Thus proteasome genes, like the RNA polymerase I1 genes (Faust et al, 1986;Bautz and Petersen. 19891, are a further example in which members of a gene family whose coordinate expression is required for enzymatic function are not located within the same chromosomal region.…”

Section: Discussionmentioning

confidence: 99%

Molecular characterization of the genomic regions of the Drosophilaα‐type submit proteasome genes PROS‐Dm28.1 and PROS‐Dm35

Frentzel¹,

Troxell²,

Haass

et al. 1992

European Journal of Biochemistry

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The proteasome (rnulticatalytic proteinase) consists of a large number of non-identical protein subunits which are encoded by the evolutionarily conserved PROS gene family. Using the PROSDm35 and PROS-Dm28.1 cDNAs as probes, we have isolated the corresponding genomic DNA clones of Drosophila melanogaster. In situ hybridization shows that the members of the PROS gene family are not organized in a single gene cluster and that, in contrast to the PROS-Dm35 gene, the PROS-Dm28.1 gene is localized on the X chromosome. Analysis of the genomic organization of the PROS-Dm28.1 and PROS-Dm35 genes reveals that both genes are interrupted by two small introns whereby the relative positions of the introns within the two coding regions are not conserved. Neither gene possesses a distinct transcriptional start site as shown by nuclease S1 analysis. Since the promoter regions also do not contain a TATA box, PROS genes appear to be typical house-keeping genes. A putative heat-shock element in the promoter region of the PROS-Dm35 gene was shown to be inactive on stress induction when fused to a reporter gene and tested in transient transfections assays. In addition, promoter deletion analysis demonstrates that the promoter region between positions -605 and -330 contains sequence elements important for PROS-Dm35 gene activity and that deletions beyond position -150 result in an almost complete inhibition of transcription.

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“…The preparation of antibodies against the RNA polymerases (3)(4)(5) has led to the isolation of the genes for some of these subunits (6,7). The largest and second-largest subunits of the three eukaryotic RNA polymerases have been found to be homologous to the ,' and ,B subunits respectively of the prokaryotic RNA polymerase (8)(9)(10)(11)(12).…”

Section: Introductionmentioning

confidence: 99%

A conjugation-specific gene (cnjC) fromTetrahymenaencodes a protein homologous to yeast RNA polymerase subunits (RPB3, RPC40) and similar to a portion of the prokaryotic RNA polymerase a subunit (rpoA)

Martindale

1990

Nucl Acids Res

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The cnjC gene from the protozoan Tetrahymena thermophila was completely sequenced. The deduced gene product was found to have significant sequence similarity to the yeast and prokaryotic RNA polymerase subunits involved with subunit assembly. Since cnjC is active only during the sexual stage (conjugation) of Tetrahymena's life cycle, these results indicate it may be part of a novel type of transcriptional control. The yeast proteins to which the Tetrahymena cnjC is homologous are the 40 kd protein of RNA polymerases I and III (coded for by gene RPC40) and the third-largest subunit of RNA polymerase II (coded for by gene RPB3). The degree of similarity of the cnjC protein to the two yeast subunits was found to be greater than the similarity of the two yeast subunits to each other. The alpha subunit of the core RNA polymerase from prokaryotes (coded for by gene rpoA) was found to have regions of similarity to the cnjC protein as well as to the subunits encoded by RPC40 and RPB3. Regions of high conservation among the four proteins are noted. The significance of these results is discussed.

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Cloning and identification of the gene coding for the 140-kd subunit of Drosophila RNA polymerase II

Cited by 15 publications

References 32 publications

RNA polymerase II subunit RPB3 is an essential component of the mRNA transcription apparatus.

RNA polymerase II subunit RPB3 is an essential component of the mRNA transcription apparatus.

Molecular characterization of the genomic regions of the Drosophilaα‐type submit proteasome genes PROS‐Dm28.1 and PROS‐Dm35

A conjugation-specific gene (cnjC) fromTetrahymenaencodes a protein homologous to yeast RNA polymerase subunits (RPB3, RPC40) and similar to a portion of the prokaryotic RNA polymerase a subunit (rpoA)

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