scholarly journals The emerging role of RNA polymerase I transcription machinery in human malignancy: a clinical perspective

2013 ◽  
pp. 909 ◽  
Author(s):  
Massimo Derenzini ◽  
Lorenzo Montanaro ◽  
Davide Treré
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase I ◽  
Clinical Perspective ◽  
Transcription Machinery ◽  
Human Malignancy ◽  
Polymerase I

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 The RNA polymerase I transcription machinery

2006 ◽  
Vol 73 ◽  
pp. 203-216 ◽  
Author(s):  
Jackie Russell ◽  
Joost C.B.M. Zomerdijk
Keyword(s):  
Rna Polymerase ◽  
Mammalian Cells ◽  
Growth Conditions ◽  
Rna Polymerase I ◽  
Cellular Growth ◽  
Rrna Synthesis ◽  
Transcription Machinery ◽  
Pol I ◽  
A Cell ◽  
Polymerase I

The rRNAs constitute the catalytic and structural components of the ribosome, the protein synthesis machinery of cells. The level of rRNA synthesis, mediated by Pol I (RNA polymerase I), therefore has a major impact on the life and destiny of a cell. In order to elucidate how cells achieve the stringent control of Pol I transcription, matching the supply of rRNA to demand under different cellular growth conditions, it is essential to understand the components and mechanics of the Pol I transcription machinery. In this review, we discuss: (i) the molecular composition and functions of the Pol I enzyme complex and the two main Pol I transcription factors, SL1 (selectivity factor 1) and UBF (upstream binding factor); (ii) the interplay between these factors during pre-initiation complex formation at the rDNA promoter in mammalian cells; and (iii) the cellular control of the Pol I transcription machinery.

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.

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