GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

YEAST:MTR4

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) MTR4 (synonyms: DOB1)
Protein Name(s) ATP-dependent RNA helicase DOB1

mRNA transport regulator MTR4

External Links
UniProt P47047
EMBL Z49325
BK006943
PIR S56822
RefSeq NP_012485.1
PDB 2XGJ
4QU4
4U4C
4WFD
PDBsum 2XGJ
4QU4
4U4C
4WFD
ProteinModelPortal P47047
SMR P47047
BioGrid 33705
DIP DIP-6394N
IntAct P47047
MINT MINT-620894
iPTMnet P47047
MaxQB P47047
PeptideAtlas P47047
EnsemblFungi YJL050W
GeneID 853397
KEGG sce:YJL050W
EuPathDB FungiDB:YJL050W
SGD S000003586
GeneTree ENSGT00820000127042
HOGENOM HOG000163047
InParanoid P47047
KO K12598
OMA HDVSYPE
OrthoDB EOG7WT48P
BioCyc YEAST:G3O-31514-MONOMER
BRENDA 3.6.4.13
Reactome [www.reactome.org/content/detail/R-SCE-6791226 R-SCE-6791226]
EvolutionaryTrace P47047
PRO PR:P47047
Proteomes UP000002311
GO GO:0005730
GO:0005634
GO:0031499
GO:0005524
GO:0034459
GO:0016491
GO:0008143
GO:0000467
GO:0043629
GO:0071031
GO:0071042
GO:0071035
GO:0071038
GO:0071049
GO:0071051
GO:0016075
GO:0034475
GO:0034476
Gene3D 3.40.50.300
InterPro IPR011545
IPR014001
IPR001650
IPR027417
IPR011254
IPR025696
IPR016438
IPR012961
Pfam PF00270
PF08148
PF00271
PF13234
PIRSF PIRSF005198
SMART SM00487
SM01142
SM00490
SUPFAM SSF52540
SSF56821
PROSITE PS51192
PS51194

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0000292

RNA fragment catabolic process

PMID:26317469[1]

ECO:0000315

P

RNA polymerase I produces pre-rRNA that is processed into several fragments, including the 5’-ETS (external transcribed spacer) and 7S pre-rRNA. The RNA exosome is a 3’ to 5’ exonuclease involved in the processing of 7S pre-rRNA into mature 5.8S rRNA and in the degradation of the 5’-ETS. The exosome requires protein cofactors that interact with the Mtr4 helicase for substrate specificity. Figure 1 F is a northern blot that shows that S. cerevisiae strains with a deletion in Mtr4’s essential arch domain accumulate 5’-ETS (lane 2). A wilde type Mtr4 strain shows that 5’ETS is degraded as it is absent on the northern blot (lane 1). Therefore, lanes 1 and 2 show that Mtr4 is involved in the breakdown of a fragment of RNA, such as excised introns or sequences removed from ribosomal RNA during processing (Go termGO:0000292)

complete
CACAO 12153

GO:0000460

maturation of 5.8S rRNA

PMID:26317469[1]

ECO:0000315

P

RNA polymerase I produces pre-rRNA that is processed into several fragments, including the 5’-ETS (external transcribed spacer) and 7S pre-rRNA. The RNA exosome is a 3’ to 5’ exonuclease involved in the processing of 7S pre-rRNA into mature 5.8S rRNA and in the degradation of the 5’-ETS. The exosome requires protein cofactors that interact with the Mtr4 helicase for substrate specificity. One of these cofactors is Nop53. The N-terminus of Nop53 is required for binding with the arch domain of Mtr4, and subsequently for presentation of the 7S pre-rRNA substrate to the RNA exosome. The northern blot in Figure 1 shows that S. cerevisiae strains with wild type Mtr4 and Nop53 accumulate no 7S-pre-rRNA. Conversely, mutants with a deletion in either the arch domain of Mtr4 or the N terminus of Nop53 show accumulation of 7S-pre-rRNA. Therefore these two proteins are involved in he maturation of a precursor 5.8S ribosomal RNA (rRNA) molecule into a mature 5.8S rRNA molecule (GO:0000460)

complete
CACAO 12154

enables

GO:0003729

mRNA binding

PMID:23222640[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0016973

poly(A)+ mRNA export from nucleus

PMID:27385342[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071051

polyadenylation-dependent snoRNA 3'-end processing

PMID:10611222[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071049

nuclear retention of pre-mRNA with aberrant 3'-ends at the site of transcription

PMID:11586364[5]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000001377

P

Seeded From UniProt

complete

involved_in

GO:0071042

nuclear polyadenylation-dependent mRNA catabolic process

PMID:19369424[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071038

nuclear polyadenylation-dependent tRNA catabolic process

PMID:18000032[7]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000005006

P

Seeded From UniProt

complete

involved_in

GO:0071038

nuclear polyadenylation-dependent tRNA catabolic process

PMID:17643380[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071038

nuclear polyadenylation-dependent tRNA catabolic process

PMID:15828860[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071038

nuclear polyadenylation-dependent tRNA catabolic process

PMID:15935758[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071035

nuclear polyadenylation-dependent rRNA catabolic process

PMID:18940861[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071035

nuclear polyadenylation-dependent rRNA catabolic process

PMID:16374505[12]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071031

nuclear mRNA surveillance of mRNA 3'-end processing

PMID:17410208[13]

ECO:0000316

genetic interaction evidence used in manual assertion

P

Seeded From UniProt

Missing: with/from

involved_in

GO:0071031

nuclear mRNA surveillance of mRNA 3'-end processing

PMID:17410208[13]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043629

ncRNA polyadenylation

PMID:15828860[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043629

ncRNA polyadenylation

PMID:15935758[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034476

U5 snRNA 3'-end processing

PMID:10508172[14]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034475

U4 snRNA 3'-end processing

PMID:10508172[14]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034475

U4 snRNA 3'-end processing

PMID:10611222[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0034459

ATP-dependent 3'-5' RNA helicase activity

PMID:18000032[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0034459

ATP-dependent 3'-5' RNA helicase activity

PMID:18096702[15]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0034459

ATP-dependent 3'-5' RNA helicase activity

PMID:18000032[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0031499

TRAMP complex

PMID:15935759[16]

ECO:0000353

physical interaction evidence used in manual assertion

SGD:S000005475

C

Seeded From UniProt

complete

part_of

GO:0031499

TRAMP complex

PMID:15935759[16]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0031499

TRAMP complex

PMID:15935758[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0031499

TRAMP complex

PMID:15828860[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0016075

rRNA catabolic process

PMID:9463390[17]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016075

rRNA catabolic process

PMID:10508172[14]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008143

poly(A) binding

PMID:18096702[15]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005730

nucleolus

PMID:16541108[18]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:15226447[19]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:8756671[20]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0000467

exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

PMID:10508172[14]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000467

exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

PMID:9463390[17]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006401

RNA catabolic process

PMID:21873635[21]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002281432
PomBase:SPAC637.11
UniProtKB:Q8IYB8

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:21873635[21]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002281442
SGD:S000003586
UniProtKB:P42285

C

Seeded From UniProt

complete

enables

GO:0004004

ATP-dependent RNA helicase activity

PMID:21873635[21]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002281432
SGD:S000005950
TAIR:locus:2130235
UniProtKB:Q8IYB8

F

Seeded From UniProt

complete

involved_in

GO:0000460

maturation of 5.8S rRNA

PMID:21873635[21]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002281442
UniProtKB:P42285

P

Seeded From UniProt

complete

enables

GO:0003676

nucleic acid binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011545

F

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016438

F

Seeded From UniProt

complete

enables

GO:0003724

RNA helicase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016438

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011254

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011545

F

Seeded From UniProt

complete

involved_in

GO:0006401

RNA catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016438

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011254

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011254

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

involved_in

GO:0006364

rRNA processing

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0698

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0004386

helicase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0347

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Thoms, M et al. (2015) The Exosome Is Recruited to RNA Substrates through Specific Adaptor Proteins. Cell 162 1029-38 PubMed GONUTS page
  2. Mitchell, SF et al. (2013) Global analysis of yeast mRNPs. Nat. Struct. Mol. Biol. 20 127-33 PubMed GONUTS page
  3. Paul, B & Montpetit, B (2016) Altered RNA processing and export lead to retention of mRNAs near transcription sites and nuclear pore complexes or within the nucleolus. Mol. Biol. Cell 27 2742-56 PubMed GONUTS page
  4. 4.0 4.1 van Hoof, A et al. (2000) Yeast exosome mutants accumulate 3'-extended polyadenylated forms of U4 small nuclear RNA and small nucleolar RNAs. Mol. Cell. Biol. 20 441-52 PubMed GONUTS page
  5. Hilleren, P et al. (2001) Quality control of mRNA 3'-end processing is linked to the nuclear exosome. Nature 413 538-42 PubMed GONUTS page
  6. Roth, KM et al. (2009) Regulation of NAB2 mRNA 3'-end formation requires the core exosome and the Trf4p component of the TRAMP complex. RNA 15 1045-58 PubMed GONUTS page
  7. 7.0 7.1 7.2 Wang, X et al. (2008) Degradation of hypomodified tRNA(iMet) in vivo involves RNA-dependent ATPase activity of the DExH helicase Mtr4p. RNA 14 107-16 PubMed GONUTS page
  8. Schneider, C et al. (2007) The exosome subunit Rrp44 plays a direct role in RNA substrate recognition. Mol. Cell 27 324-31 PubMed GONUTS page
  9. 9.0 9.1 9.2 Vanácová, S et al. (2005) A new yeast poly(A) polymerase complex involved in RNA quality control. PLoS Biol. 3 e189 PubMed GONUTS page
  10. 10.0 10.1 10.2 LaCava, J et al. (2005) RNA degradation by the exosome is promoted by a nuclear polyadenylation complex. Cell 121 713-24 PubMed GONUTS page
  11. Callahan, KP & Butler, JS (2008) Evidence for core exosome independent function of the nuclear exoribonuclease Rrp6p. Nucleic Acids Res. 36 6645-55 PubMed GONUTS page
  12. Houseley, J & Tollervey, D (2006) Yeast Trf5p is a nuclear poly(A) polymerase. EMBO Rep. 7 205-11 PubMed GONUTS page
  13. 13.0 13.1 Rougemaille, M et al. (2007) Dissecting mechanisms of nuclear mRNA surveillance in THO/sub2 complex mutants. EMBO J. 26 2317-26 PubMed GONUTS page
  14. 14.0 14.1 14.2 14.3 Allmang, C et al. (1999) Functions of the exosome in rRNA, snoRNA and snRNA synthesis. EMBO J. 18 5399-410 PubMed GONUTS page
  15. 15.0 15.1 Bernstein, J et al. (2008) Characterization of the essential activities of Saccharomyces cerevisiae Mtr4p, a 3'->5' helicase partner of the nuclear exosome. J. Biol. Chem. 283 4930-42 PubMed GONUTS page
  16. 16.0 16.1 Wyers, F et al. (2005) Cryptic pol II transcripts are degraded by a nuclear quality control pathway involving a new poly(A) polymerase. Cell 121 725-37 PubMed GONUTS page
  17. 17.0 17.1 de la Cruz, J et al. (1998) Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for the 3' end formation of 5.8S rRNA in Saccharomyces cerevisiae. EMBO J. 17 1128-40 PubMed GONUTS page
  18. Dez, C et al. (2006) Surveillance of nuclear-restricted pre-ribosomes within a subnucleolar region of Saccharomyces cerevisiae. EMBO J. 25 1534-46 PubMed GONUTS page
  19. Pertschy, B et al. (2004) Diazaborine treatment of yeast cells inhibits maturation of the 60S ribosomal subunit. Mol. Cell. Biol. 24 6476-87 PubMed GONUTS page
  20. Liang, S et al. (1996) A DEAD-box-family protein is required for nucleocytoplasmic transport of yeast mRNA. Mol. Cell. Biol. 16 5139-46 PubMed GONUTS page
  21. 21.0 21.1 21.2 21.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page