scholarly journals Role of the RNA/DNA kinase Grc3 in transcription termination by RNA polymerase I

EMBO Reports ◽  
2010 ◽  
Vol 11 (10) ◽  
pp. 758-764 ◽  
Author(s):  
Priscilla Braglia ◽  
Katrin Heindl ◽  
Alexander Schleiffer ◽  
Javier Martinez ◽  
Nick J Proudfoot
Keyword(s):  
Rna Polymerase ◽  
Transcription Termination ◽  
Rna Polymerase I ◽  
Polymerase I

scholarly journals Role of Second-Largest RNA Polymerase I Subunit Zn-Binding Domain in Enzyme Assembly

2003 ◽  
Vol 2 (5) ◽  
pp. 1046-1052 ◽  
Author(s):  
Tatyana Naryshkina ◽  
Adrian Bruning ◽  
Olivier Gadal ◽  
Konstantin Severinov
Keyword(s):  
Rna Polymerase ◽  
Binding Domain ◽  
Rna Polymerases ◽  
Rna Polymerase I ◽  
Cysteine Residues ◽  
Per Se ◽  
Essential Function ◽  
Polymerase I

ABSTRACT The second-largest subunits of eukaryal RNA polymerases are similar to the β subunits of prokaryal RNA polymerases throughout much of their lengths. The second-largest subunits from eukaryal RNA polymerases contain a four-cysteine Zn-binding domain at their C termini. The domain is also present in archaeal homologs but is absent from prokaryal homologs. Here, we investigated the role of the C-terminal Zn-binding domain of Rpa135, the second-largest subunit of yeast RNA polymerase I. Analysis of nonfunctional Rpa135 mutants indicated that the Zn-binding domain is required for recruitment of the largest subunit, Rpa190, into the RNA polymerase I complex. Curiously, the essential function of the Rpa135 Zn-binding domain is not related to Zn2+ binding per se, since replacement of only one of the four cysteine residues with alanine led to the loss of Rpa135 function. Even more strikingly, replacement of all four cysteines with alanines resulted in functional Rpa135.

The Role of Mammalian SL1 in Promoter Selective Transcriptional Regulation of RNA Polymerase I

1999 ◽  
Vol 27 (3) ◽  
pp. A98-A98
Author(s):  
J Karsten Friedrich ◽  
Kostya I Panov ◽  
Pavel Cabart ◽  
Joost CBM Zomerdijk
Keyword(s):  
Transcriptional Regulation ◽  
Rna Polymerase ◽  
Rna Polymerase I ◽  
Polymerase I

scholarly journals Two RNA Polymerase I Subunits Control the Binding and Release of Rrn3 during Transcription

2007 ◽  
Vol 28 (5) ◽  
pp. 1596-1605 ◽  
Author(s):  
Frédéric Beckouet ◽  
Sylvie Labarre-Mariotte ◽  
Benjamin Albert ◽  
Yukiko Imazawa ◽  
Michel Werner ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Transcription Initiation ◽  
Binding Domain ◽  
Rna Polymerase I ◽  
Initiation Factor ◽  
C Terminus ◽  
Transcription Initiation Factor ◽  
Polymerase I ◽  
Polymerase Mutants

ABSTRACT Rpa34 and Rpa49 are nonessential subunits of RNA polymerase I, conserved in species from Saccharomyces cerevisiae and Schizosaccharomyces pombe to humans. Rpa34 bound an N-terminal region of Rpa49 in a two-hybrid assay and was lost from RNA polymerase in an rpa49 mutant lacking this Rpa34-binding domain, whereas rpa34Δ weakened the binding of Rpa49 to RNA polymerase. rpa34Δ mutants were caffeine sensitive, and the rpa34Δ mutation was lethal in a top1Δ mutant and in rpa14Δ, rpa135(L656P), and rpa135(D395N) RNA polymerase mutants. These defects were shared by rpa49Δ mutants, were suppressed by the overexpression of Rpa49, and thus, were presumably mediated by Rpa49 itself. rpa49 mutants lacking the Rpa34-binding domain behaved essentially like rpa34Δ mutants, but strains carrying rpa49Δ and rpa49-338::HIS3 (encoding a form of Rpa49 lacking the conserved C terminus) had reduced polymerase occupancy at 30°C, failed to grow at 25°C, and were sensitive to 6-azauracil and mycophenolate. Mycophenolate almost fully dissociated the mutant polymerase from its ribosomal DNA (rDNA) template. The rpa49Δ and rpa49-338::HIS3 mutations had a dual effect on the transcription initiation factor Rrn3 (TIF-IA). They partially impaired its recruitment to the rDNA promoter, an effect that was bypassed by an N-terminal deletion of the Rpa43 subunit encoded by rpa43-35,326, and they strongly reduced the release of the Rrn3 initiation factor during elongation. These data suggest a dual role of the Rpa49-Rpa34 dimer during the recruitment of Rrn3 and its subsequent dissociation from the elongating polymerase.

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