RNA polymerase III transcription

Stefano, J. E., Purified lupus antigen La recognizes an oligouridylate stretch common to the 3 termini of RNA polymerase III transcripts. Cell 36, 145-154 (1984). 

Another direct comparison between the photophores, although not in an activity-based setting, was reported by Tate and coworkers [87]. They synthesized dUTP analogs containing four different photoreactive moieties 84a-d (Fig. 9a) and incorporated them enzymatically into DNA constructs. With these, the DNA PAL of yeast RNA polymerase III transcription complexes was studied. It was shown that photolabeling with the diazirine construct (84d) rendered many protein-DNA contacts, whereas labeling with the other three photoreactive moieties (84a-c) proved only marginal. 

Zinc-fingers are common in DNA-binding proteins of eukaryotes but are not found in prokaryotes. Examples of zinc-finger proteins include the RNA polymerase III transcription factor TFIIIA, steroid receptors, and some gene products that control development. The zinc-finger consists of pairs of cysteine and/or histidine residues within an a-helix. These residues bind tightly to a Zn2+ ion, which allows the a-helical amino acids to interact with specific sequences. See Figure 12-18. 

Goodfellow SJ, White RJ. 2007. Regulation of RNA polymerase III transcription during mammalian cell growth. Cell Cycle 6 2323-2326. 

Nascently transcribed eukaryotic iRNAs are among the most processed of all RNA polymerase III transcripts. Like those of prokaryotic tRNAs, the 5 leader is cleaved by RNase P, the 3 trailer is removed, and CCA is added by the CCA-adding enzyme (Figure 29.25). Eukaryotic tRNAs are also heavily modified on base and ribose moieties these modifications are important for function. In contrast with prokaryotic tRNAs, many eukaryotic pre-tRNAs are also spliced by an endonuclease and a ligase to remove an intron. 

See also RNA Polymerase I Transcription, RNA Polymerase III Transcription, RNA Polymerase II Transcription, Chromatin Structure and Transcription, Eukaryotic Transcription. Termination of Eukaryotic Transcription, Chromatin Remodeling, Transcription Factor Binding Domains... 

RNA Polymerase III Transcription of Small RNA Genes (Figure 28.21, Figure 28.22, Figure 28.23)... 

Baker, R. E., Gabrielsen, O., and Hall, B. D. (1986). Effects of tRNATyr point mutations on the binding of yeast RNA polymerase III transcription factor C. J. Biol. Chem. 261, 5275-5282. 

Colbert, T., and Hahn, S. (1992). A yeast TFIIB related factor involved in RNA polymerase III transcription. Genes Dev. 6, 1940-1949. 

Felton-Edkins, Z. A., and White, R. J. (2002). Multiple mechanisms contribute to the activation of RNA polymerase III transcription in cells transformed by papova-viruses./ Biol. Chem. ill, 48182-48191. 

Huang, Y., and Maraia, R. J. (2001). Comparison of the RNA polymerase III transcription machinery in Schizosaccharomyces pombe, Saccharomyces cerevisiae and human. Nucleic Acids Res. 29, 2675-2690. 

Kassavetis, G. A., Bardeleben, C., Kumar, A., Ramirez, E., and Geiduschek, E. P. (1997). Domains of the Brf component of RNA polymerase III transcription factor IIIB (TFIIIB) functions in assembly of TFIIIB-DNA complexes and recruitment of RNA polymerase to the promoter. Mol. Cell. Biol. 17, 5299-5306. 

Kassavetis, G. A., Joazeiro, C. A., Pisano, M., Geiduschek, E. P., Colbert, T., Hahn, S., and Blanco, J. A. (1992). The role of the TATA-binding protein in the assembly and function of the multisubunit yeast RNA polymerase III transcription factor, TFIIIB. Cell 71, 1055-1064. 

Lopez-de-Leon, A., Librizzi, M., Puglia, K., and Willis, I. M. (1992). PCF4 encodes an RNA polymerase III transcription factor with homology to TFIIB. Cell 7211-220. 

Mital, R., Kobayashi, R., and Hernandez, N. (1996). RNA polymerase III transcription from the human U6 and adenovirus type 2 VAI promoters has different requirements for human BRF, a subunit of human TFIIIB. Mol. Cell. Biol. 16, 7031-7042. 

Upadhya, R., Lee, J., and Willis, I. M. (2002). Mafl Is an essential mediator of diverse signals that repress RNA polymerase III transcription. Mol. Cell 10, 1489-1494. Wang, Z and Roeder, R. G. (1995). Structure and function of a human transcription... 

White, R. J. (1998a). RNA Polymerase III Transcription. 2nd ed., Springer, New York. White, R. J. (1998b). Transcription factor IIIB An important determinant of biosynthetic capacity that is targeted by tumour suppressors and transforming proteins. 

MysUnski E, Ame JC, Krol A, Carbon P (2001) An unusually compact external promoter for RNA polymerase III transcription of the human HIRNA gene. Nucleic Acids Res 29 2502-2509. 

Anti-SS-B/La 47-kDa phosphoprotein complexed with RNA polymerase III transcripts SS, neonatal lupus, SLE... 

This system provided the first opportunity to test whether the VSV wt leader is the viral product responsible for the inhibition of the initiation of DNA-dependent RNA synthesis. Later studies (McGowan and Wagner, unpublished data) indicate that, when DNA templates transcribed by RNA polymerase II and III in vitro are used simultaneously in the same reaction, polymerase II activity is inhibited more easily than RNA polymerase III transcripts, confirming previous in vivo data obtained by Week and Wagner (1978, 1979 ). 

Shen, C.-K., and Maniatis, T., 1982, The organization, structure, and in vitro transcription of the ALU family RNA polymerase III transcription units in the human a-like globin gene cluster Precipitation of in vitro transcripts by lupus and La antibodies, J. Mol. Appl. Gen. 1 343. 

In addition to the early and late genes that are expressed as mRNA and are transcribed by the host cells RNA polymerase form II, the adenoviral genome encodes two small RNA species, termed VA-RNAi and VA-RNAu. These viral genes are transcribed by RNA polymerase III. Transcription of both occurs during the early phase of infection, but that of the VA-RNAi gene accelerates once an infection enters the late phase (Soderlund et al., 1976). Indeed, VA-RNAi is produced in much larger quantities than VA-RNAn and accumulates in the cytoplasm (Mathews and Pettersson, 1978), where it is essential for the efficient translation of viral mRNA species (Thimmappaya et al., 1982). 

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