ArticleMolecular and cellular biology1998
Interactions within the yeast Sm core complex: from proteins to amino acids.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 49 citations in OpenAlex.
- Screening of selected ageing-related proteins that extend chronological life span in yeast Saccharomyces cerevisiae.Scientific reports · 2021Article
- A Novel Model of Tumor-Infiltrating B Lymphocyte Specific RNA-Binding Protein-Related Genes With Potential Prognostic Value and Therapeutic Targets in Multiple Myeloma.Frontiers in genetics · 2021Article
- Reconstructing genome-wide protein-protein interaction networks using multiple strategies with homologous mapping.PloS one · 2015Article
- Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome.PeerJ · 2013Article
- Time-course proteome analysis reveals the dynamic response of Cryptococcus gattii cells to fluconazole.PloS one · 2012Article
- Identification of genes associated with local aggressiveness and metastatic behavior in soft tissue tumors.Translational oncology · 2010Article
- A map of human protein interactions derived from co-expression of human mRNAs and their orthologs.Molecular systems biology · 2008Article
- Sm core variation in spliceosomal small nuclear ribonucleoproteins from Trypanosoma brucei.The EMBO journal · 2006Article
- Depletion of SMN by RNA interference in HeLa cells induces defects in Cajal body formation.Nucleic acids research · 2006Article
- Sequence-structure-function relationships of Tgs1, the yeast snRNA/snoRNA cap hypermethylase.Nucleic acids research · 2003Article
- The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci.RNA (New York, N.Y.) · 2002Article
- A conserved Drosophila transportin-serine/arginine-rich (SR) protein permits nuclear import of Drosophila SR protein splicing factors and their antagonist repressor splicing factor 1.Molecular biology of the cell · 2002Article
- Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein.RNA (New York, N.Y.) · 2001Article
- RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex.The EMBO journal · 2001Article
- The Sm domain is an ancient RNA-binding motif with oligo(U) specificity.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Functional characterization of nuclear localization signals in yeast Sm proteins.Molecular and cellular biology · 2000Article
- The spliceosomal snRNP core complex of Trypanosoma brucei: cloning and functional analysis reveals seven Sm protein constituents.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Genome-wide protein interaction screens reveal functional networks involving Sm-like proteins.Yeast (Chichester, England) · 2000Article
- A Sm-like protein complex that participates in mRNA degradation.The EMBO journal · 2000Article
- Herpesvirus mRNAs are sorted for export via Crm1-dependent and -independent pathways.Journal of virology · 2000Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sm core proteins play an essential role in the formation of small nuclear ribonucleoprotein particles (snRNPs) by binding to small nuclear RNAs and participating in a network of protein interactions. The two-hybrid system was used to identify SmE interacting proteins and to test for interactions between all pairwise combinations of yeast Sm proteins. We observed interactions between SmB and SmD3, SmE and SmF, and SmE and SmG. For these interactions, a direct biochemical assay confirmed the validity of the results obtained in vivo. To map the protein-protein interaction surface of Sm proteins, we generated a library of SmE mutants and investigated their ability to interact with SmF and/or SmG proteins in the two-hybrid system. Several classes of mutants were observed: some mutants are unable to interact with either SmF or SmG proteins, some interact with SmG but not with SmF, while others interact moderately with SmF but not with SmG. Our mutational analysis of yeast SmE protein shows that conserved hydrophobic residues are essential for interactions with SmF and SmG as well as for viability. Surprisingly, we observed that other evolutionarily conserved positions are tolerant to mutations, with substitutions affecting binding to SmF and SmG only mildly and conferring a wild-type growth phenotype.
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