scholarly journals A Chimeric Subunit of Yeast Transcription Factor IIIC Forms a Subcomplex with τ95

1998 ◽  
Vol 18 (6) ◽  
pp. 3191-3200 ◽  
Author(s):  
Nathalie Manaud ◽  
Rosalía Arrebola ◽  
Bénédicte Buffin-Meyer ◽  
Olivier Lefebvre ◽  
Hartmut Voss ◽  
...  

ABSTRACT The multisubunit yeast transcription factor IIIC (TFIIIC) is a multifunctional protein required for promoter recognition, transcription factor IIIB recruitment, and chromatin antirepression. We report the isolation and characterization of TFC7, an essential gene encoding the 55-kDa polypeptide, τ55, present in affinity-purified TFIIIC. τ55 is a chimeric protein generated by an ancient chromosomal rearrangement. Its C-terminal half is essential for cell viability and sufficient to ensure TFIIIC function in DNA binding and transcription assays. The N-terminal half is nonessential and highly similar to a putative yeast protein encoded on another chromosome and to a cyanobacterial protein of unknown function. Partial deletions of the N-terminal domain impaired τ55 function at a high temperature or in media containing glycerol or ethanol, suggesting a link between PolIII transcription and metabolic pathways. Interestingly, τ55 was found, together with TFIIIC subunit τ95, in a protein complex which was distinct from TFIIIC and which may play a role in the regulation of PolIII transcription, possibly in relation to cell metabolism.

1998 ◽  
Vol 18 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Rosalía Arrebola ◽  
Nathalie Manaud ◽  
Sophie Rozenfeld ◽  
Marie-Claude Marsolier ◽  
Olivier Lefebvre ◽  
...  

ABSTRACT Transcription factor IIIC (TFIIIC) (or τ) is a large multisubunit and multifunctional factor required for transcription of all class III genes in Saccharomyces cerevisiae. It is responsible for promoter recognition and TFIIIB assembly. We report here the cloning and characterization of TFC6, an essential gene encoding the 91-kDa polypeptide, τ91, present in affinity-purified TFIIIC. τ91 has a predicted molecular mass of 74 kDa. It harbors a central cluster of His and Cys residues and has basic and acidic amino acid regions, but it shows no specific similarity to known proteins or predicted open reading frames. The TFIIIC subunit status of τ91 was established by the following biochemical and genetic evidence. Antibodies to τ91 bound TFIIIC-DNA complexes in gel shift assays; in vivo, a B block-deficient U6 RNA gene (SNR6) harboring GAL4 binding sites was reactivated by fusing the GAL4 DNA binding domain to τ91; and a point mutation in TFC6 (τ91-E330K) was found to suppress the thermosensitive phenotype of a tfc3-G349Emutant affected in the B block binding subunit (τ138). The suppressor mutation alleviated the DNA binding and transcription defects of mutant TFIIIC in vitro. These results indicated that τ91 cooperates with τ138 for DNA binding. Recombinant τ91 by itself did not interact with a tRNA gene, although it showed a strong affinity for single-stranded DNA.


Gene ◽  
1996 ◽  
Vol 174 (2) ◽  
pp. 221-224 ◽  
Author(s):  
Travis Henry ◽  
Brian Kliewer ◽  
Robert Palmatier ◽  
Joseph S. Ulphani ◽  
Joe D. Beckmann

2011 ◽  
Vol 30 (3) ◽  
pp. 679-689 ◽  
Author(s):  
Lei Liu ◽  
Xiao-Lu Cao ◽  
Rui Bai ◽  
Na Yao ◽  
Lu-Bin Li ◽  
...  

1994 ◽  
Vol 205 (2) ◽  
pp. 1250-1256 ◽  
Author(s):  
K. Ogura ◽  
T. Nishiyama ◽  
A. Hiratsuka ◽  
T. Watabe ◽  
T. Watabe

Gene ◽  
1990 ◽  
Vol 91 (2) ◽  
pp. 225-232 ◽  
Author(s):  
Judit Castella-Escola ◽  
David M. Ojcius ◽  
Philippe LeBoulch ◽  
Virginie Joulin ◽  
Yves Blouquit ◽  
...  

2013 ◽  
Vol 23 (1) ◽  
pp. 42-51 ◽  
Author(s):  
Ibandalin Mawlong ◽  
Kishwar Ali ◽  
Devika Kurup ◽  
Sangita Yadav ◽  
Aruna Tyagi

Viruses ◽  
2022 ◽  
Vol 14 (1) ◽  
pp. 108
Author(s):  
Wang Liu ◽  
Xiaowei Zheng ◽  
Xin Dai ◽  
Zhenfeng Zhang ◽  
Wenyan Zhang ◽  
...  

Viruses are far more abundant than cellular microorganisms in the marine ecosystem. However, very few viruses have so far been isolated from marine sediments, especially hydrothermal vent sediments, hindering the understanding of the biology and ecological functions of these tiny organisms. Here, we report the isolation and characterization of a temperate bacteriophage, named PVJ1, which infects Psychrobacillus from a hydrothermal vent field in Okinawa Trough. PVJ1 belongs to the Myoviridae family of the order Caudovirales. The tailed phage possesses a 53,187 bp linear dsDNA genome, with 84 ORFs encoding structural proteins, genome replication, host lysis, etc. in a modular pattern. The phage genome is integrated into the host chromosome near the 3′-end of deoD, a gene encoding purine nucleoside phosphorylase (PNP). The phage integration does not appear to disrupt the function of PNP. The phage DNA is packaged by the headful mechanism. Release of PVJ1 from the host cell was drastically enhanced by treatment with mitomycin C. Phages encoding an MCP sharing significant similarity (≥70% identical amino acids) with that of PVJ1 are widespread in diverse environments, including marine and freshwater sediments, soils, artificial ecosystems, and animal intestines, and primarily infect Firmicutes. These results are valuable to the understanding of the lifestyle and host interactions of bacterial viruses at the bottom of the ocean.


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