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Dynamic association of capping enzymes with transcribing RNA polymerase II.
It is shown that yeast capping enzymes cross-link in vivo to the 5' ends of transcribed genes and that this localization requires the C-terminal heptad repeat domain (CTD).
Prp43 Is an Essential RNA-dependent ATPase Required for Release of Lariat-Intron from the Spliceosome*
- Arnold Martin, S. Schneider, B. Schwer
- Medicine, BiologyThe Journal of Biological Chemistry
- 17 May 2002
A new ATP-dependent step of splicing that is catalyzed by Prp43 is defined, and it is shown that the lariat-intron is not accessible to debranching by purified Dbr1 when it is held in the T123A-arrested splicing complex.
Ntr1 activates the Prp43 helicase to trigger release of lariat-intron from the spliceosome.
It is reported that activation of Prp43's inherently feeble helicase activity by the splicing factor Ntr1 is required for lariat-intron release and demonstrated for the first time that regulating the motor activity of a DEAH-box protein by an accessory factor is critical for mRNA splicing.
Prp22, a DExH‐box RNA helicase, plays two distinct roles in yeast pre‐mRNA splicing
Prp22 has two distinct functions in yeast pre‐mRNA splicing: an ATP‐independent role during the second catalytic step and an ATP-requiring function in disassembly of the spliceosome.
A conformational rearrangement in the spliceosome sets the stage for Prp22-dependent mRNA release.
- B. Schwer
- Biology, MedicineMolecular cell
- 20 June 2008
The findings support a model for Prp 22-catalyzed mRNA release from the spliceosome wherein a rearrangement that accompanies the second transesterification step deposits Prp22 on the mRNA downstream of the exon-exon junction.
PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome
The splicing factor PRP16 has been purified and shown to exhibit RNA-dependent ATPase activity, suggesting that it may be the prototype for a set of splicing factors which use ATP to drive a cycle of conformational changes.
How Slu7 and Prp18 cooperate in the second step of yeast pre-mRNA splicing.
It is shown that the 382-amino-acid Slu7 protein contains two functionally important domains: a zinc knuckle (122CRNCGEAGHKEKDC135) and a Prp18-interaction domain (215EIELMKLELY224) that are important for cooperation in splicing.
RNA capping enzyme and DNA ligase: a superfamily of covalent nucleotidyl transferases
It is proposed that the cellular and DNA virus capping enzymes and ATP‐dependent ligases constitute a protein superfamily evolved from a common ancestral enzyme, and more extensive similarity to the ligases than they do to the poxvirus cappers.
TFIIH and P-TEFb coordinate transcription with capping enzyme recruitment at specific genes in fission yeast.
- Laia Viladevall, Courtney V St Amour, +7 authors R. P. Fisher
- Biology, MedicineMolecular cell
- 27 March 2009
It is proposed that TFIIH primes the CTD and promotes recruitment of P-TEFb/Pcm1, serving to couple elongation and capping of select pre-mRNAs, servingTo define their functions, theTFIIH-associated kinase Mcs6 and P- TEFb homologs Cdk9 and Lsk1 of fission yeast were mutated, making them sensitive to inhibition by bulky purine analogs.
A conformational rearrangement in the spliceosome is dependent on PRP16 and ATP hydrolysis.
It is demonstrated that PRP16 can hydrolyse all nucleoside triphosphates and corresponding deoxynucleotides; complementation of the second catalytic step shows the same broad nucleotide specificity.