SUS1 Sus1p [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SUS1
Official Full Name: Sus1p
Primary source: SGD:S000028510
Locus tag: YBR111W-A
See related: AllianceGenome:SGD:S000028510; FungiDB:YBR111W-A; VEuPathDB:YBR111W-A
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables enzyme activator activity. Involved in several processes, including RNA metabolic process; histone modification; and poly(A)+ mRNA export from nucleus. Located in nucleoplasm. Part of nucleus. Orthologous to human ENY2 (ENY2 transcription and export complex 2 subunit). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See SUS1 in Genome Data Viewer

Location:: chromosome: II

Exon count:: 3

Sequence:: Chromosome: II; NC_001134.8 (462139..462579)

Chromosome II - NC_001134.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001134.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Study portrays the biophysical characterization of Sus1 from S. cerevisiae. Sus1 protein is a alpha-helical structure which is stable at various pH conditions. The results reported the alpha-helix to beta-sheet transition at low pH as well as at high pH. Also, Sus1 secondary structure was found to be stable till 55% alcohol concentration while tertiary structure was stable up to 20% concentration.
Title: An insight into structural plasticity and conformational transitions of transcriptional co-activator Sus1.
Study provides support for a model in which SAGA/TREX-2 factor Sus1 acts as a global transcriptional regulator in yeast but has differential activity at yeast genes as a function of their transcription rate or during stress conditions.
Title: The SAGA/TREX-2 subunit Sus1 binds widely to transcribed genes and affects mRNA turnover globally.
results provide solid evidence for a role of Sus1 in negatively regulating telomere length through the modulation of H2BK123 mono-ubiquitination and its interaction with the nuclear pore complex
Title: The evolutionarily conserved factor Sus1/ENY2 plays a role in telomere length maintenance.
Exon three-way junction structure exerted a role in SUS1 transcript metabolism that includes splicing and transcript degradation.
Title: An exon three-way junction structure modulates splicing and degradation of the SUS1 yeast pre-mRNA.
Examination of pre-mRNA splicing efficiency in these mutants reveals the requirement of Npl3 methylation for the efficient splicing of SUS1 intron 1, but not of ECM33 or ASC1.
Title: Protein arginine methylation of Npl3 promotes splicing of the SUS1 intron harboring non-consensus 5' splice site and branch site.
Study described the formation of mutually exclusive complexes of ENY2 with insulator proteins and Sgfl1-a component of the SAGA complex, direct binding partner for ENY2
Title: CTCF and Sgfl1 proteins form alternative complexes with ENY2 proteins.
demonstrates that I2 structure is relevant for SUS1 expression, and that this effect is likely exerted through modulation of splicing
Title: An intronic RNA structure modulates expression of the mRNA biogenesis factor Sus1.
Nonsense-mediated decay pathway and the splicing factor Mud2 both play a role in SUS1 expression.
Title: SUS1 introns are required for efficient mRNA nuclear export in yeast.
the pattern of SUS1 splicing changes in response to environmental change such as temperature elevation, and the retained intron product is subject to nonsense-mediated decay.
Title: Key features of the two-intron Saccharomyces cerevisiae gene SUS1 contribute to its alternative splicing.
study reports the 1.90 angstrom resolution crystal structure of the deubiquitinating module (DUBm)- which contains Ubp8 bound to Sgf11, Sus1 and Sgf73- bound to ubiquitin aldehyde, as well as the 2.45 angstrom resolution structure of the uncomplexed DUBm
Title: Structural insights into the assembly and function of the SAGA deubiquitinating module.

Submit: New GeneRIF Correction See all GeneRIFs (14)

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 chromatin binding	IBA Inferred from Biological aspect of Ancestor more info
enables chromatin binding	IDA Inferred from Direct Assay more info	PubMed
enables enzyme activator activity	IDA Inferred from Direct Assay more info	PubMed
enables transcription coactivator activity	IBA Inferred from Biological aspect of Ancestor more info
enables transcription coactivator activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in chromatin organization	IEA Inferred from Electronic Annotation more info
involved_in mRNA export from nucleus	IEA Inferred from Electronic Annotation more info
involved_in mRNA transport	IEA Inferred from Electronic Annotation more info
involved_in nuclear mRNA surveillance	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in poly(A)+ mRNA export from nucleus	IBA Inferred from Biological aspect of Ancestor more info
involved_in poly(A)+ mRNA export from nucleus	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of DNA-templated transcription	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of transcription by RNA polymerase II	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein transport	IEA Inferred from Electronic Annotation more info
involved_in regulation of protein localization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of transcription by RNA polymerase II	IBA Inferred from Biological aspect of Ancestor more info
involved_in transcription elongation by RNA polymerase II	IEA Inferred from Electronic Annotation more info
involved_in transcription elongation by RNA polymerase II	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of DUBm complex	IBA Inferred from Biological aspect of Ancestor more info
part_of DUBm complex	IDA Inferred from Direct Assay more info	PubMed
part_of DUBm complex	IEA Inferred from Electronic Annotation more info
located_in P-body	IEA Inferred from Electronic Annotation more info
part_of SAGA complex	IBA Inferred from Biological aspect of Ancestor more info
part_of SAGA complex	IDA Inferred from Direct Assay more info	PubMed
part_of SAGA complex	IEA Inferred from Electronic Annotation more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
part_of nuclear pore	IDA Inferred from Direct Assay more info	PubMed
part_of nuclear pore	IEA Inferred from Electronic Annotation more info
located_in nucleoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in nucleoplasm	IEA Inferred from Electronic Annotation more info
located_in nucleus	IEA Inferred from Electronic Annotation more info
part_of transcription export complex 2	IDA Inferred from Direct Assay more info	PubMed
part_of transcription export complex 2	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Sus1p

NP_878049.2

Global transcriptional regulator, component of SAGA, TREX-2 complexes; interacts with RNA polymerase II; involved in mRNA export coupled transcription activation and elongation; involved in post-transcriptional tethering of active genes to nuclear periphery and to non-nascent mRNP; plays role in negatively regulating telomere length through modulation of H2BK123 mono-ubiquitination and its interaction with nuclear pore complex