The purified yeast pre-mRNA splicing factor PRP2 is an RNA-dependent NTPase.

Kim, Sahn Ho; Smith, Joseph L.; Claude, Alejandro; Lin, Ren‐Jang

doi:10.1002/j.1460-2075.1992.tb05291.x

Cited by 140 publications

(106 citation statements)

References 35 publications

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“…3A, column 6), consistent with the fact that Prp2 has a broad rNTP specificity (Kim et al 1992). As yeast Brr2 is strictly ATP-specific, it is very unlikely that Brr2 ATPase activity is involved in the displacement of Cwc24 from the spliceosome, suggesting that this dissociation is solely due to the action of Prp2.…”

Section: Generation Of Doubly Labeled Spliceosomes For Dcfccs Measuresupporting

confidence: 57%

Prp2-mediated protein rearrangements at the catalytic core of the spliceosome as revealed by dcFCCS

Ohrt¹,

Prior²,

Dannenberg³

et al. 2012

RNA

132

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The compositional and conformational changes during catalytic activation of the spliceosome promoted by the DEAH box ATPase Prp2 are only poorly understood. Here, we show by dual-color fluorescence cross-correlation spectroscopy (dcFCCS) that the binding affinity of several proteins is significantly changed during the Prp2-mediated transition of precatalytic B act spliceosomes to catalytically activated B* spliceosomes from Saccharomyces cerevisiae. During this step, several proteins, including the zinc-finger protein Cwc24, are quantitatively displaced from the B* complex. Consistent with this, we show that Cwc24 is required for step 1 but not for catalysis per se. The U2-associated SF3a and SF3b proteins Prp11 and Cus1 remain bound to the B* spliceosome under near-physiological conditions, but their binding is reduced at high salt. Conversely, high-affinity binding sites are created for Yju2 and Cwc25 during catalytic activation, consistent with their requirement for step 1 catalysis. Our results suggest high cooperativity of multiple Prp2-mediated structural rearrangements at the spliceosome's catalytic core. Moreover, dcFCCS represents a powerful tool ideally suited to study quantitatively spliceosomal protein dynamics in equilibrium.

show abstract

Section: Generation Of Doubly Labeled Spliceosomes For Dcfccs Measuresupporting

confidence: 57%

Prp2-mediated protein rearrangements at the catalytic core of the spliceosome as revealed by dcFCCS

Ohrt¹,

Prior²,

Dannenberg³

et al. 2012

RNA

132

View full text Add to dashboard Cite

show abstract

“…13 Consequently, a glutamine coordinated to the N6 and N7 positions of adenine as well as a hydrophobic group stacking on the base may be a recurring theme in ATP-dependent SF1 and SF2 helicases. This would imply that SF1 and SF2 helicases that lack this conserved glutamine might be nonspecific NTPases, and this seems to be the case with the viral helicase NS3 14 and the DEAH box helicases Prp2 15 and Prp16. 16,17 Moreover, many of the hexameric superfamilies (SF3, F4, F5) of helicases lack a strict nucleotide preference for binding.…”

Section: The Newly Identified Q Motif Of Dead Box Helicases Is Involvmentioning

confidence: 99%

The Newly Identified Q Motif of DEAD Box Heicases IS Involved in Adenine Recognition

Tanner¹

2003

Cell Cycle

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“…PRP2 and PRP16 both exhibit nonspecific RNA-binding activity and hydrolyze ATP when single-stranded RNA is provided (Schwer and Guthrie 1991;Kim et al 1992). PRP2 is required for the 5' cleavage reaction in splicing (Kim and Lin 1993), and PRPl6 for 3' cleavage (Schwer and Guthrie 1991).…”

Section: Hls Contains Homology To Rna-dependent Atpasesmentioning

confidence: 99%

Homeless is required for RNA localization in Drosophila oogenesis and encodes a new member of the DE-H family of RNA-dependent ATPases.

Gillespie¹,

Berg²

1995

Genes Dev.

154

151

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The homeless (hls) gene of Drosophila is required for anteroposterior and dorsoventral axis formation during oogenesis. At a low frequency, females homozygous for mutations in hls generate early egg chambers in which the oocyte is positioned incorrectly within the cyst. At a high frequency, late-stage egg chambers exhibit a ventralized chorion. Sequence analysis of the hls cDNA predicts a protein with amino-terminal homology to members of the DE-H family of RNA-dependent ATPases and putative helicases. Similarity of 51% in the amino-terminal third of the protein was found to two yeast splicing factors, PRP2 and PRP16, and to Drosophila Maleless, which is required for dosage compensation. To analyze Hls function, RNA localization patterns were determined for seven different transcripts in hls mutant ovaries. Previtellogenic transport to the oocyte was unaffected for all transcripts examined. Transport and localization of bicoid and oskm messages during vitellogenic stages were strongly disrupted, and the distribution and/or quantity of gurken, orb, and fs(3)KIO mRNAs were also affected, but to a lesser degree. In contrast, hu-li tai shao and Biicaudul-D transcripts were transported and localized normally in hls mutants. In addition, Kinesin heavy chain:p-Galactosidase fusion protein failed to localize correctly to the posterior of the oocyte in vitellogenic egg chambers. Examination of the microtubule structure with anti-a-Tubulin antibodies revealed aberrant microtubule organizing center movement and an abnormally dense cytoplasmic microtubule meshwork. We discuss potential roles for Hls in organizing a cytoskeletal framework essential for localizing specific RNAs.

show abstract

The purified yeast pre-mRNA splicing factor PRP2 is an RNA-dependent NTPase.

Cited by 140 publications

References 35 publications

Prp2-mediated protein rearrangements at the catalytic core of the spliceosome as revealed by dcFCCS

Prp2-mediated protein rearrangements at the catalytic core of the spliceosome as revealed by dcFCCS

The Newly Identified Q Motif of DEAD Box Heicases IS Involved in Adenine Recognition

Homeless is required for RNA localization in Drosophila oogenesis and encodes a new member of the DE-H family of RNA-dependent ATPases.

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