LSM1 Lsm1p [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: LSM1
Official Full Name: Lsm1p
Primary source: SGD:S000003660
Locus tag: YJL124C
See related: AllianceGenome:SGD:S000003660; FungiDB:YJL124C; VEuPathDB:YJL124C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: SPB8
Summary: Enables chromatin binding activity and mRNA binding activity. Involved in deadenylation-dependent decapping of nuclear-transcribed mRNA. Located in P-body and nucleus. Part of Lsm1-7-Pat1 complex. Orthologous to human LSM1 (LSM1 homolog, mRNA degradation associated). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See LSM1 in Genome Data Viewer

Location:: chromosome: X

Exon count:: 1

Sequence:: Chromosome: X; NC_001142.9 (187126..187644, complement)

Chromosome X - NC_001142.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001142.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Our results define the roles of Pat1, Lsm1, and Dhh1 in decapping of general mRNAs and suggest that these factors may monitor mRNA translation and target unique features of individual mRNAs.
Title: General decapping activators target different subsets of inefficiently translated mRNAs.
Study observations indicate that Saccharomyces cerevisiae Pat1 and Lsm1 are important for dampening ribosome transit in the 5'-UTR, and thus translation initiation of osmostress mRNAs, in particular under low stress conditions.
Title: The Lsm1-7/Pat1 complex binds to stress-activated mRNAs and modulates the response to hyperosmotic shock.
P-bodies like LSM1 form in response to stress and act as sites of mRNA storage and degradation. Here the authors identify the mRNA targets of P-bodies during DNA replication stress, and show that P-body proteins act to prevent toxic accumulation of these target transcripts.
Title: P-body proteins regulate transcriptional rewiring to promote DNA replication stress resistance.
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
Title: Mutagenic Analysis of the C-Terminal Extension of Lsm1.
The middle domain of Pat1 is essential for the interaction of Pat1 with the Lsm1-7 complex in vivo.
Title: Pat1 contributes to the RNA binding activity of the Lsm1-7-Pat1 complex.
LSm1, Pat1, and Dhh1 control the RNA3/RNA1 ratio of Flock House virus RNAs.
Title: The cellular decapping activators LSm1, Pat1, and Dhh1 control the ratio of subgenomic to genomic Flock House virus RNAs.
The authors identify histone mRNAs as substrates of the Lsm1-7-Pat1 complex in yeast, and show that abnormally high amounts of histones accumulate in lsm1Delta mutant cells.
Title: Lsm1 promotes genomic stability by controlling histone mRNA decay.
LSM1 over-expression in the yeast Saccharomyces cerevisiae inhibits growth primarily due to U6 snRNA depletion, thereby altering pre-mRNA splicing.
Title: LSM1 over-expression in Saccharomyces cerevisiae depletes U6 snRNA levels.
Results describe a range of mutant and hybrid Lsm1 and Lsm8 proteins, shedding light on the relative importance of their various domains in determining their localization and ability to support growth.
Title: Analysis of Lsm1p and Lsm8p domains in the cellular localization of Lsm complexes in budding yeast.
Lsmlp may confer protection against UV-radiation damage by protecting the 3' ends of mRNAs from exosome-dependent 3' to 5' degradation as part of a novel RAD5-mediated, PCNA-K164 ubiquitylation-independent subpathway of PRR.
Title: A role for Lsmlp in response to ultraviolet-radiation damage in Saccharomyces cerevisiae.

Submit: New GeneRIF Correction See all GeneRIFs (12)

Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables RNA binding	IEA Inferred from Electronic Annotation more info
enables chromatin binding	IDA Inferred from Direct Assay more info	PubMed
enables mRNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables mRNA binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in deadenylation-dependent decapping of nuclear-transcribed mRNA	IBA Inferred from Biological aspect of Ancestor more info
involved_in deadenylation-dependent decapping of nuclear-transcribed mRNA	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mRNA processing	IEA Inferred from Electronic Annotation more info
involved_in nuclear-transcribed mRNA catabolic process	IEA Inferred from Electronic Annotation more info
involved_in nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of Lsm1-7-Pat1 complex	IBA Inferred from Biological aspect of Ancestor more info
part_of Lsm1-7-Pat1 complex	IDA Inferred from Direct Assay more info	PubMed
is_active_in P-body	IBA Inferred from Biological aspect of Ancestor more info
located_in P-body	IDA Inferred from Direct Assay more info	PubMed
located_in P-body	IEA Inferred from Electronic Annotation more info
located_in P-body	IMP Inferred from Mutant Phenotype more info	PubMed
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info
part_of protein-containing complex	IEA Inferred from Electronic Annotation more info
part_of ribonucleoprotein complex	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Lsm1p

NP_012411.1

Lsm (Like Sm) protein; forms heteroheptameric complex (with Lsm2p, Lsm3p, Lsm4p, Lsm5p, Lsm6p, and Lsm7p) involved in degradation of cytoplasmic mRNAs; also enters the nucleus and positively regulates transcription initiation; unlike most Sm-like proteins, Lsm1p requires both its SM-domain and C-terminal domain for RNA-binding; binds to mRNAs under glucose starvation, most often in the 3' UTR; forms cytoplasmic foci upon DNA replication stress