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Gene Review:

MUD2 - Mud2p

Saccharomyces cerevisiae S288c

Synonyms: Splicing factor MUD2, YKL074C, YKL358

Wang, Q. et al., Kistler, A.L. et al., Görnemann, J. et al., Abovich, N. et al., Fortes, P. et al., et al.

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High impact information on MUD2

We tested the predictions that the yeast UAP56 homolog, SUB2, is required for the same step and functions collaboratively with MUD2, the yeast homolog of U2AF65 [1].
The yeast MUD2 protein: an interaction with PRP11 defines a bridge between commitment complexes and U2 snRNP addition [2].
The experiments identify a specific inter-snRNP protein-protein contact that occurs during spliceosome assembly and more generally support substantial functional similarity between U2AF65 and MUD2P [2].
In vivo commitment to splicing in yeast involves the nucleotide upstream from the branch site conserved sequence and the Mud2 protein [3].
A directed two-hybrid screen reveals a network of prospective interactions that includes previously unreported intra-SF3b contacts and SF3b interactions with the RES subunit Bud13p, the Prp5p DExD/H-box protein, Mud2p, and the late-acting nineteen complex [4].

Biological context of MUD2

Moreover, deletion of MUD2 exacerbates the cs phenotype of sub2 alleles yet suppresses both the ts sub2-1 and the lethal Deltasub2 phenotypes [1].
Accumulation of the U1, U2, and U5 small nuclear ribonucleoprotein particles (snRNPs) and the 3' splice site binding factors Mud2p and BBP was detected in patterns indicative of progressive and complete spliceosome assembly; recruitment of the nineteen complex (NTC) component Prp19p suggests that splicing catalysis is also cotranscriptional [5].
The U2 snRNP promotes prespliceosome assembly through interactions that minimally involve the branchpoint binding protein, Mud2p, and the pre-mRNA [4].
Transient interaction of BBP/ScSF1 and Mud2 with the splicing machinery affects the kinetics of spliceosome assembly [6].

Physical interactions of MUD2

We propose that Sub2 functionally interacts with Mud2 both before and after PS formation [1].

Other interactions of MUD2

Physical interaction of yCBC with the commitment complex components Mud10p and Mud2p, which may directly mediate yCBC function, was demonstrated [7].

References

Deletion of MUD2, the yeast homolog of U2AF65, can bypass the requirement for sub2, an essential spliceosomal ATPase. Kistler, A.L., Guthrie, C. Genes Dev. (2001) [Pubmed]
The yeast MUD2 protein: an interaction with PRP11 defines a bridge between commitment complexes and U2 snRNP addition. Abovich, N., Liao, X.C., Rosbash, M. Genes Dev. (1994) [Pubmed]
In vivo commitment to splicing in yeast involves the nucleotide upstream from the branch site conserved sequence and the Mud2 protein. Rain, J.C., Legrain, P. EMBO J. (1997) [Pubmed]
Interactions of the yeast SF3b splicing factor. Wang, Q., He, J., Lynn, B., Rymond, B.C. Mol. Cell. Biol. (2005) [Pubmed]
Cotranscriptional spliceosome assembly occurs in a stepwise fashion and requires the cap binding complex. Görnemann, J., Kotovic, K.M., Hujer, K., Neugebauer, K.M. Mol. Cell (2005) [Pubmed]
Transient interaction of BBP/ScSF1 and Mud2 with the splicing machinery affects the kinetics of spliceosome assembly. Rutz, B., Séraphin, B. RNA (1999) [Pubmed]
Genetic and physical interactions involving the yeast nuclear cap-binding complex. Fortes, P., Kufel, J., Fornerod, M., Polycarpou-Schwarz, M., Lafontaine, D., Tollervey, D., Mattaj, I.W. Mol. Cell. Biol. (1999) [Pubmed]

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AGOS_ADR130W	Ashbya gossypii ATCC 10895
KLLA0F26433g	Kluyveromyces lactis NRRL Y-1140

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