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• W2330237189 abstract "The first atomic structures of RNAP III bring novel insight into the mechanisms that promote efficient synthesis of short RNAs. A loose active center, tight DNA-binding cleft, and other features will drive experiments to target RNA synthesis in cancer. A crystal structure of Brf2 with type 3 promoter DNA uncovered a novel switch mechanism for selenocysteine tRNA synthesis and control of the oxidative stress response. The dimethyl-G26 modification found on some tRNAs is linked to RNAP III and regulated by Maf1, which is conserved from yeast to human. Because dimethyl-G26 increases tRNA activity for decoding, it alters cellular mRNA translational profiles. Mutations throughout the two largest RNAP III subunits cause the developmental neurological disorder hypomyelinating leukodystrophy (HLD). These mutations likely decrease tRNA synthesis, affect dimethyl-G26, and alter mRNA translation. RNA synthesis in eukaryotes is divided among three RNA polymerases (RNAPs). RNAP III transcribes hundreds of tRNA genes and fewer additional short RNA genes. We survey recent work on transcription by RNAP III including an atomic structure, mechanisms of action, interactions with chromatin and retroposons, and a conserved link between its activity and a tRNA modification that enhances mRNA decoding. Other new work suggests important mechanistic connections to oxidative stress, autoimmunity and cancer, embryonic stem cell pluripotency, and tissue-specific developmental effects. We consider that, for some of its complex functions, variation in RNAP III activity levels lead to nonuniform changes in tRNAs that can shift the translation profiles of key codon-biased mRNAs with resultant phenotypes or disease states. RNA synthesis in eukaryotes is divided among three RNA polymerases (RNAPs). RNAP III transcribes hundreds of tRNA genes and fewer additional short RNA genes. We survey recent work on transcription by RNAP III including an atomic structure, mechanisms of action, interactions with chromatin and retroposons, and a conserved link between its activity and a tRNA modification that enhances mRNA decoding. Other new work suggests important mechanistic connections to oxidative stress, autoimmunity and cancer, embryonic stem cell pluripotency, and tissue-specific developmental effects. We consider that, for some of its complex functions, variation in RNAP III activity levels lead to nonuniform changes in tRNAs that can shift the translation profiles of key codon-biased mRNAs with resultant phenotypes or disease states." @default.
• W2330237189 created "2016-06-24" @default.
• W2330237189 creator A5049076723 @default.
• W2330237189 creator A5053624950 @default.
• W2330237189 date "2016-06-01" @default.
• W2330237189 modified "2023-10-08" @default.
• W2330237189 title "RNA Polymerase III Advances: Structural and tRNA Functional Views" @default.
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