Mutagenic Analysis of the C-Terminal Extension of Lsm1

• Published in: PloS one Vol. 11; no. 7; p. e0158876
• Main Authors: Chowdhury, Ashis, Kalurupalle, Swathi, Tharun, Sundaresan
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 19.07.2016; Public Library of Science (PLoS)
• Subjects: Analysis; Binding; Biochemistry; Biology and life sciences; Decay rate; Engineering and Technology; Eukaryotes; Experiments; Gene expression; Health sciences; Humans; LSm proteins; Molecular Conformation; mRNA turnover; Multiprotein Complexes - chemistry; Multiprotein Complexes - genetics; Mutagenesis - genetics; Mutation; Mutation - genetics; Nucleic Acid Denaturation - genetics; Plasmids; Protection and preservation; Protein Binding; Proteins; Research and analysis methods; Residues; Ribonucleic acid; RNA; RNA Cap-Binding Proteins - chemistry; RNA Cap-Binding Proteins - genetics; RNA Stability; RNA-Binding Proteins - chemistry; RNA-Binding Proteins - genetics; Saccharomyces cerevisiae; Saccharomyces cerevisiae - chemistry; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - genetics; United States > US
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0158876

The Sm-like proteins (also known as Lsm proteins) are ubiquitous in nature and exist as hexa or heptameric RNA binding complexes. They are characterized by the presence of the Sm-domain. The Lsm1 through Lsm7 proteins are highly conserved in eukaryotes and they form a hetero-octameric complex together with the protein Pat1. The Lsm1-7-Pat1 complex plays a key role in mRNA decapping and 3'-end protection and therefore is required for normal mRNA decay rates in vivo. Lsm1 is a key subunit that is critical for the unique RNA binding properties of this complex. We showed earlier that unlike most Sm-like proteins, Lsm1 uniquely requires both its Sm domain and its C-terminal extension to contribute to the function of the Lsm1-7-Pat1 complex and that the C-terminal segment can associate with the rest of the complex and support the function even in trans. The studies presented here identify a set of residues at the very C-terminal end of Lsm1 to be functionally important and suggest that these residues support the function of the Lsm1-7-Pat1 complex by facilitating RNA binding either directly or indirectly.