The RNA polymerase I subunit Rpa12p interacts with the stress-responsive transcription factor Msn4p to regulate lipid metabolism in budding yeast

FEBS Letters ◽  
2016 ◽  
Vol 590 (20) ◽  
pp. 3559-3573 ◽  
Author(s):  
Kamlesh Kumar Yadav ◽  
Neelima Singh ◽  
Praveen Kumar Rajvanshi ◽  
Ram Rajasekharan
Keyword(s):  
Transcription Factor ◽  
Lipid Metabolism ◽  
Rna Polymerase ◽  
Budding Yeast ◽  
Rna Polymerase I ◽  
Polymerase I ◽  
Regulate Lipid Metabolism

scholarly journals Characterization of a Novel Class I Transcription Factor A (CITFA) Subunit That Is Indispensable for Transcription by the Multifunctional RNA Polymerase I of Trypanosoma brucei

2012 ◽  
Vol 11 (12) ◽  
pp. 1573-1581 ◽  
Author(s):  
Tu N. Nguyen ◽  
Bao N. Nguyen ◽  
Ju Huck Lee ◽  
Aswini K. Panigrahi ◽  
Arthur Günzl
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase ◽  
Trypanosoma Brucei ◽  
Rna Polymerase I ◽  
Class I ◽  
Mammalian Host ◽  
Subunit Structure ◽  
Content Type ◽  
Pol I ◽  
Polymerase I

ABSTRACT Trypanosoma brucei is the only organism known to have evolved a multifunctional RNA polymerase I (pol I) system that is used to express the parasite's ribosomal RNAs, as well as its major cell surface antigens, namely, the variant surface glycoprotein (VSG) and procyclin, which are vital for establishing successful infections in the mammalian host and the tsetse vector, respectively. Thus far, biochemical analyses of the T. brucei RNA pol I transcription machinery have elucidated the subunit structure of the enzyme and identified the class I transcription factor A (CITFA). CITFA binds to RNA pol I promoters, and its CITFA-2 subunit was shown to be absolutely essential for RNA pol I transcription in the parasite. Tandem affinity purification (TAP) of CITFA revealed the subunits CITFA-1 to -6, which are conserved only among kinetoplastid organisms, plus the dynein light chain DYNLL1. Here, by tagging CITFA-6 instead of CITFA-2, a complex was purified that contained all known CITFA subunits, as well as a novel proline-rich protein. Functional studies carried out in vivo and in vitro , as well as a colocalization study, unequivocally demonstrated that this protein is a bona fide CITFA subunit, essential for parasite viability and indispensable for RNA pol I transcription of ribosomal gene units and the active VSG expression site in the mammalian-infective life cycle stage of the parasite. Interestingly, CITFA-7 function appears to be species specific, because expression of an RNA interference (RNAi)-resistant CITFA-7 transgene from Trypanosoma cruzi could not rescue the lethal phenotype of silencing endogenous CITFA-7 .

scholarly journals The RNA Polymerase I Transcription Factor UBF Is the Product of a Primary Response Gene

1995 ◽  
Vol 270 (9) ◽  
pp. 4209-4212 ◽  
Author(s):  
Marija Glibetic ◽  
Laura Taylor ◽  
Dawn Larson ◽  
Ross Hannan ◽  
Bruce Sells ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase ◽  
Primary Response ◽  
Rna Polymerase I ◽  
Response Gene ◽  
Primary Response Gene ◽  
Polymerase I

scholarly journals A New Strategy of RNA Interference That Targets Heterologous Sequences Reveals CITFA1 as an Essential Component of Class I Transcription Factor A in Trypanosoma brucei

2014 ◽  
Vol 13 (6) ◽  
pp. 785-795 ◽  
Author(s):  
Sung Hee Park ◽  
Bao N. Nguyen ◽  
Justin K. Kirkham ◽  
Tu N. Nguyen ◽  
Arthur Günzl
Keyword(s):  
Transcription Factor ◽  
Rna Interference ◽  
Rna Polymerase ◽  
Trypanosoma Brucei ◽  
Transcription Initiation ◽  
Single Copy ◽  
Rna Polymerase I ◽  
Class I ◽  
Content Type ◽  
Polymerase I

ABSTRACTConditional gene silencing by RNA interference inTrypanosoma bruceican be inconclusive if knockdowns are inefficient or have off-target effects. To enable efficient, specific silencing of single-copy genes in mammalian-infective, bloodstream form trypanosomes, we developed a system that targets the heterologous and functionalTrypanosoma cruziU2AF353′ untranslated region (UTR) (Tc3) or, alternatively, the sequence of the PTP tag, which can be fused to any mRNA of interest. Two cell lines were created, single-marker Tc3 (smTc3) and smPTP, which conditionally express Tc3 and PTP double-stranded RNA (dsRNA), respectively. The system depends on manipulating both alleles of the gene of interest so that cells exclusively express the target mRNA as a fusion to one of these heterologous sequences. We generated allele integration vectors in which the C-terminal part of a gene's coding sequence can be fused to either heterologous sequence in a single cloning step. We first tested this system withCITFA7, which encodes a well-characterized subunit of the class I transcription factor A (CITFA), an essential factor for transcription initiation by RNA polymerase I. Targeting either Tc3 or PTP fused to theCITFA7mRNA resulted in gene knockdowns that were as efficient and specific as targeting the endogenousCITFA7mRNA. Moreover, application of this system toCITFA1, which could not be silenced by established methods, demonstrated that the gene encodes an essential CITFA subunit that mediates binding of the transcription factor complex to RNA polymerase I promoters.

scholarly journals The fission yeast RPA51 is a functional homolog of the budding yeast A49 subunit of RNA polymerase I and required for maximizing transcription of ribosomal DNA

2003 ◽  
Vol 78 (3) ◽  
pp. 199-209 ◽  
Author(s):  
Kaori Nakagawa ◽  
Koji Hisatake ◽  
Yukiko Imazawa ◽  
Akira Ishiguro ◽  
Masahito Matsumoto ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Fission Yeast ◽  
Ribosomal Dna ◽  
Budding Yeast ◽  
Rna Polymerase I ◽  
Functional Homolog ◽  
Polymerase I

rUBF, an RNA polymerase I transcription factor from rats, produces DNase I footprints identical to those produced by xUBF, its homolog from frogs

1990 ◽  
Vol 10 (7) ◽  
pp. 3810-3812
Author(s):  
C S Pikaard ◽  
S D Smith ◽  
R H Reeder ◽  
L Rothblum
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Rna Polymerase ◽  
Affinity Purification ◽  
Binding Specificity ◽  
Rna Polymerase I ◽  
Dna Binding Specificity ◽  
Apparent Homogeneity ◽  
And Function ◽  
Polymerase I

Rat cells contain a DNA-binding polymerase I transcription factor, rUBF, with properties similar to UBF homologs that have been purified from both human (hUBF) and frog (xUBF) cells. In this note we report the affinity purification of rUBF to apparent homogeneity and show that UBFs from both rat and frog have identical footprinting characteristics on templates from either species. Furthermore, xUBF was able to stimulate transcription from rat RNA polymerase I promoters in a partially fractionated rat extract that was UBF dependent. These results strengthen the conclusion that all vertebrate cells contain a UBF homolog whose DNA-binding specificity and function have been strongly conserved.

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