Linked Life Data

10749973

Source:http://linkedlifedata.com/resource/pubmed/id/10749973

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2000-6-1
pubmed:databankReference
pubmed:abstractText
The motor neuron disease spinal muscular atrophy (SMA) is caused by reduced levels of functional survival of motor neurons (SMN) protein. Previous studies have shown that SMN binds to the SMN-interacting protein SIP1 and mediates the assembly of spliceosomal U snRNPs in the cytoplasm. In addition, a nuclear function for SMN in pre-mRNA splicing has recently been proposed. Here, we describe the analysis of the Schizo-saccharomyces pombe protein Yab8p and provide evidence that it is structurally and functionally related to SMN found in higher eukaryotes. We show that Yab8p interacts via its N-terminus with a novel protein termed Yip1p. Importantly, Yip1p exhibits homology to SIP1, and the mode of binding to Yab8p is remarkably similar to the SMN-SIP1 interaction. Hence, Yip1p is likely to be the homologue of SIP1 in S.pombe. Yab8p and Yip1p localize predominantly in the nucleus. Genetic studies demonstrate that Yab8p is essential for viability. Strikingly, suppression of YAB8 expression in a conditional knock-out strain causes nuclear accumulation of poly(A) mRNA and inhibition of splicing. These data identify Yab8p as a novel factor involved in splicing and suggest that Yab8p exerts a function similar or identical to the nuclear pool of SMN. Our studies provide a model system to study the cellular function of SMN in yeast, and should help in understanding the molecular events leading to SMA.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0964-6906
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
663-74
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10749973-Amino Acid Sequence, pubmed-meshheading:10749973-Animals, pubmed-meshheading:10749973-Base Sequence, pubmed-meshheading:10749973-Cell Nucleus, pubmed-meshheading:10749973-Cloning, Molecular, pubmed-meshheading:10749973-Cyclic AMP Response Element-Binding Protein, pubmed-meshheading:10749973-DNA, Complementary, pubmed-meshheading:10749973-DNA Primers, pubmed-meshheading:10749973-Fungal Proteins, pubmed-meshheading:10749973-Genes, Essential, pubmed-meshheading:10749973-Humans, pubmed-meshheading:10749973-Molecular Sequence Data, pubmed-meshheading:10749973-Nerve Tissue Proteins, pubmed-meshheading:10749973-Protein Binding, pubmed-meshheading:10749973-RNA, Messenger, pubmed-meshheading:10749973-RNA-Binding Proteins, pubmed-meshheading:10749973-SMN Complex Proteins, pubmed-meshheading:10749973-Schizosaccharomyces, pubmed-meshheading:10749973-Schizosaccharomyces pombe Proteins, pubmed-meshheading:10749973-Sequence Homology, Amino Acid
pubmed:year
2000
pubmed:articleTitle
The Schizosaccharomyces pombe protein Yab8p and a novel factor, Yip1p, share structural and functional similarity with the spinal muscular atrophy-associated proteins SMN and SIP1.
pubmed:affiliation
Max-Planck-Institute for Biochemistry, Am Klopferspitz 18a, D-82152 Martinsried, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't