Protein interactions in nuclear pre-mRNA splicing in Saccharomyces cerevisiae

Jamieson, Derek J.; Whittaker, Erica; King, David S.; Anderson, Gordon J.; Beggs, Jean D.

doi:10.1007/bf00360449

Molecular Biology Reports

1990

DOI: 10.1007/bf00360449

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Protein interactions in nuclear pre-mRNA splicing in Saccharomyces cerevisiae

Derek J. Jamieson

Erica Whittaker

David S. King

et al.

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1996

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“…Moreover, it has been shown that human U2 snRNA can substitute for yeast U2 snRNA (41). All of these data indicate that the overall features of U2 snRNP are conserved from yeasts to humans, and yeast counterparts of mammalian U2AЈ and U2BЉ proteins are likely to exist.Genetic tools have been successfully employed with S. cerevisiae to identify and study splicing factors (14,15). Through the characterization of temperature-sensitive mutants and their suppressors, several U2 snRNP-associated factors (e.g., Prp9p, Prp11p, and Prp21p) have been cloned and characterized (2,18,35,44).…”

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Identification and Characterization of a Yeast Gene Encoding the U2 Small Nuclear Ribonucleoprotein Particle B″ Protein

Tang

Abovich

Rosbash

1996

Molecular and Cellular Biology

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The inessential yeast gene MUD2 encodes a protein factor that contributes to U1 small nuclear ribonucleoprotein particle (snRNP)-pre-mRNA complex (commitment complex) formation. To identify other genes that contribute to this early splicing step, we performed a synthetic lethal screen with a MUD2 deletion strain. The first characterized gene from this screen, MSL1 (MUD synthetic lethal 1), encodes the yeast homolog of the well studied mammalian snRNP protein U2B؆. The yeast protein (YU2B؆) is a component of yeast U2 snRNP, and it is related to other members of the U1A-U2B؆ family, the human U2B؆ protein, the human U1A protein, and the yeast U1A protein. It binds in vitro to its RNA target, U2 snRNA stem-loop IV, without a protein cofactor, and the target resembles more closely the U1 snRNA binding site of the human U1A protein than it does the U2 snRNA binding site of human U2B؆. Surprisingly, the YU2B؆ protein lacks a C-terminal RNA binding domain, which is conserved in all other family members. Possible functional and evolutionary relationships among these proteins are discussed.The removal of introns from eukaryotic pre-mRNAs takes place in large complexes called spliceosomes. Spliceosomes are assembled on pre-mRNA in an ordered pathway that includes the addition of protein factors and four small nuclear ribonucleoprotein particles (snRNPs), U1, U2, U5, and U4/U6 snRNPs. U1 snRNP recognizes the 5Ј splice site, U2 binds to the branch point, and the U4/U5/U6 tri-snRNP is subsequently added to form a catalytic complex (9,24,26,28,29).Extensive biochemical studies of metazoan splicing snRNPs have led to the characterization of their components. Each snRNP has one or two snRNAs, several specific proteins, and eight core Sm proteins common to all four snRNPs (26, 37). These biochemical studies as well as molecular cloning have shown that U2 snRNP contains two specific proteins, U2BЉ and U2AЈ (10, 42). U2BЉ belongs to a large family of RNA-binding proteins which share a conserved motif, the RNA binding domain (RBD) (5, 16). In association with U2AЈ, U2BЉ binds to U2 snRNA stem-loop IV with high affinity (6, 36).In the yeast Saccharomyces cerevisiae, the general mechanism and machinery of splicing are quite similar to those in mammals. Although yeast U2 snRNA is six times larger than mammalian U2 snRNA, the sequences and structures of important regions of the molecule are conserved. These include the branch point recognition site, the Sm binding site, and stem-loop IV (3). Much of the ''extra'' sequence can be removed from the yeast U2 snRNA with little or no consequence, e.g., the molecule functions well with an internal deletion of about 900 nucleotides (27,40). Moreover, it has been shown that human U2 snRNA can substitute for yeast U2 snRNA (41). All of these data indicate that the overall features of U2 snRNP are conserved from yeasts to humans, and yeast counterparts of mammalian U2AЈ and U2BЉ proteins are likely to exist.Genetic tools have been successfully employed with S. cerevisiae to identify and study spl...

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confidence: 99%

Identification and Characterization of a Yeast Gene Encoding the U2 Small Nuclear Ribonucleoprotein Particle B″ Protein

Tang

Abovich

Rosbash

1996

Molecular and Cellular Biology

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Protein interactions in nuclear pre-mRNA splicing in Saccharomyces cerevisiae

Cited by 1 publication

References 15 publications

Identification and Characterization of a Yeast Gene Encoding the U2 Small Nuclear Ribonucleoprotein Particle B″ Protein

Identification and Characterization of a Yeast Gene Encoding the U2 Small Nuclear Ribonucleoprotein Particle B″ Protein

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