Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related system that resembles bacterial sulfur transfer systems. - Wikidata - wikimedia - TriplyDB

Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related system that resembles bacterial sulfur transfer systems.

Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related system that resembles bacterial sulfur transfer systems.

http://www.wikidata.org/entity/Q27933952

about

A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways Origin and function of ubiquitin-like proteins Multiple Layers of Stress-Induced Regulation in tRNA Biology Biosynthesis and functions of sulfur modifications in tRNA Prokaryotic ubiquitin-like protein modification Defects in tRNA modification associated with neurological and developmental dysfunctions in Caenorhabditis elegans elongator mutants Crystallographic and mutational studies on the tRNA thiouridine synthetase TtuA A genetic interaction map of RNA-processing factors reveals links between Sem1/Dss1-containing complexes and mRNA export and splicing Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier.Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions.Multiple TORC1-associated proteins regulate nitrogen starvation-dependent cellular differentiation in Saccharomyces cerevisiae.The dual role of ubiquitin-like protein Urm1 as a protein modifier and sulfur carrier Crystallization and preliminary X-ray analysis of the yeast tRNA-thiouridine modification protein 1 (Tum1p)Urm1 at the crossroad of modifications. 'Protein Modifications: Beyond the Usual Suspects' Review Series tRNA biology charges to the front Unexpected accumulation of ncm(5)U and ncm(5)S(2) (U) in a trm9 mutant suggests an additional step in the synthesis of mcm(5)U and mcm(5)S(2)U Allele-specific suppressors of lin-1(R175Opal) identify functions of MOC-3 and DPH-3 in tRNA modification complexes in Caenorhabditis elegans Urm1 couples sulfur transfer to ubiquitin-like protein function in oxidative stress The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans E1- and ubiquitin-like proteins provide a direct link between protein conjugation and sulfur transfer in archaea.Modification of tRNA(Lys) UUU by elongator is essential for efficient translation of stress mRNAs.tRNA thiolation links translation to stress responses in Saccharomyces cerevisiae.Functional importance of Ψ38 and Ψ39 in distinct tRNAs, amplified for tRNAGln(UUG) by unexpected temperature sensitivity of the s2U modification in yeast Abbreviated Pathway for Biosynthesis of 2-Thiouridine in Bacillus subtilis Uncovering ubiquitin and ubiquitin-like signaling networks.Optimization of Codon Translation Rates via tRNA Modifications Maintains Proteome Integrity.Posttranslational modification of cellular proteins by a ubiquitin-like protein in bacteria.Arabidopsis molybdopterin biosynthesis protein Cnx5 collaborates with the ubiquitin-like protein Urm11 in the thio-modification of tRNA.Ubiquitin-like proteins and their roles in archaea.Elongator-dependent modification of cytoplasmic tRNALysUUU is required for mitochondrial function under stress conditions.tRNA tKUUU, tQUUG, and tEUUC wobble position modifications fine-tune protein translation by promoting ribosome A-site binding.Sulfur amino acids regulate translational capacity and metabolic homeostasis through modulation of tRNA thiolation.Elp3 links tRNA modification to IRES-dependent translation of LEF1 to sustain metastasis in breast cancer Archaeal ubiquitin-like SAMP3 is isopeptide-linked to proteins via a UbaA-dependent mechanism.Thiolated tRNAs of Trypanosoma brucei are imported into mitochondria and dethiolated after import.The putative tRNA 2-thiouridine synthetase Ncs6 is an essential sulfur carrier in Methanococcus maripaludis.Bacterial cysteine desulfurases: versatile key players in biosynthetic pathways of sulfur-containing biofactors.The natural history of ubiquitin and ubiquitin-related domains.Elongator, a conserved complex required for wobble uridine modifications in eukaryotes.

P2860

06ad402c62db91e6369f653123806cb11a1f0abe 0d80b057eae3999b8abb4c3de9df3704d4a717eb 21fc22846d2808fbfc1c3dca91fc1ebd013a1410 2fcd223cb33993212e0fccecacdf02e441875e9b 48187c882afd9fd48416d2ce0319b2c7d5a01bdf 57bf7cc5d61a0f2c72aa633337c636054ec3924b 6226037c8becd949acd2b97199ae4e60287324c7 7596b7e1bf2e77ad47f13bdf74a2f869ed4c65cd 828a7656596895eb24b459188b800ffd3a1d3a2b a40401ecb3b8e87b18fd469b519fee51485d124a a5919195fd7e6068e39a83883f6ec91d80479c2c bad9b53cba14b023c89095ccc991327095f1be9a e163aafe48f5764a1a5bd1616881986a660a8902 e51820e039d23ac21af5ab1dfc203b9b72ca52c0 e6f82586e9d4bbbab86e87c02c6500f932ea7036 f501f9f9582a146c12419ca1f0411ef89c263e3e

P248

Q24315993-D28DEF63-B5FB-42AC-83E3-9FDBE9ABFAB4 Q24647626-CFD464C0-9D93-467A-92FA-CC6042823046 Q24651141-CF7F49F8-B1F6-4217-9EF7-C7073BD3D396 Q26749584-7D721C52-825D-43DC-B6DA-19C9C6D66125 Q26851281-152722C4-7C20-4CCB-9AA2-8E7A05283DD5 Q26998484-E72AE131-1683-41D9-BAC0-E0DB4500F056 Q27312120-550374C2-E1B3-4F17-802D-8277917BC13A Q27684090-1A866F00-AEF7-4E38-B7BB-2B4446C58E00 Q27932638-138EECD6-3FA1-4542-931F-3A3322296A43 Q27932686-3FE606F8-5A37-47EE-A2BB-2C12957E3641 Q27935445-DDAC42BC-22E6-449F-A022-6C066DEC1EF3 Q27935833-815B35A5-2E10-4694-B89C-6FD8F3134979 Q28602413-436A9010-4B23-4B7C-8080-B78D19380C9D Q28741740-45294427-57DB-4F75-8256-7FC10E947B64 Q28756158-A34EA0BE-9F7C-45DE-978E-FF3BF9210619 Q29616318-D308BEFB-04CD-44D2-A285-AA022C3D2193 Q33936919-A4E31A77-0072-49B1-8BF0-9052A1427176 Q34082199-0FC7F22A-A42E-4BD9-9595-22B9552D23B3 Q34159673-09AB4873-36DE-4146-BDE4-7D02172D188C Q34674294-CD8BD1A7-4126-4A49-8173-DB6F7DB3EC55 Q34693707-EDA87043-2C97-413D-AA6C-997B6C83087A Q34846015-D2B8B019-0747-45E7-A7E0-F91270E13320 Q34960691-9F385B6F-AA00-47CB-A77A-C8C925B6F5A0 Q35113613-2B5A5940-9B83-4C82-B875-177C09ED5F60 Q35572964-A508A7F3-469C-4671-AC72-5AF75345F9AF Q35615172-C0D81F03-5CA2-4120-9A5F-41F209F41646 Q35855945-761EC37B-20AC-4BA8-B388-58ED46293B65 Q36006888-1A36BFD6-B89E-47BC-86BB-D67A940A0E23 Q36216527-57E73711-BD26-4645-9956-988E70BAF721 Q36501230-9AC73606-4BA1-4B5F-BC85-CF602338964B Q36676640-15888314-27B9-4789-8A18-6A39EF8942A4 Q37049384-7A76D7AA-6079-401C-A303-4C59E3D985C8 Q37133127-254619CD-4F17-44D0-BBEA-170151D88D9E Q37346677-4EAAC4D5-0EF8-45D1-99A3-32C4F9CA8532 Q37428832-F1909273-2CB6-4046-8D61-CF1FF70575DD Q37479396-2D46B819-30AE-4E45-984B-3807D71FA008 Q37695718-0837DC5D-D9F9-4BCD-8D1A-69A3842BAC05 Q37878385-BD71753E-7C7D-46D8-95CE-AEB19FD5C30D Q37971572-C943EDF1-61C6-4C2E-BEB3-00BF63507538 Q38326905-2F8626E9-5D94-4989-9E7D-5B36507C5DB2

P2860

Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related system that resembles bacterial sulfur transfer systems.

http://www.wikidata.org/entity/Q27933952

description

2008 nî lūn-bûn

@nan

2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Thio-modification of yeast cyt ...... erial sulfur transfer systems.

@ast

Thio-modification of yeast cyt ...... erial sulfur transfer systems.

@en

Thio-modification of yeast cyt ...... erial sulfur transfer systems.

@nl

type

label

Thio-modification of yeast cyt ...... erial sulfur transfer systems.

@ast

Thio-modification of yeast cyt ...... erial sulfur transfer systems.

@en

Thio-modification of yeast cyt ...... erial sulfur transfer systems.

@nl

prefLabel

Thio-modification of yeast cyt ...... erial sulfur transfer systems.

@ast

Thio-modification of yeast cyt ...... erial sulfur transfer systems.

@en

Thio-modification of yeast cyt ...... erial sulfur transfer systems.

@nl

P1433

Q27933952-5AA6BE7C-96DA-4AF4-BE23-D60CB55DFD9A

P1476

Q27933952-2A1D58BA-FA14-48AA-85C6-CA6D0DC086E7

P2093

Q27933952-7E25B1ED-154F-4F2E-9E3E-9094DBAD3BBD

Q27933952-DCD85CE7-EFA3-4221-94EA-831AEB0E032A

Q27933952-E496E423-1CA4-4ED5-9BF7-EC4879A0C981

P2860

Q27933952-03F3B78C-C2A8-4ED7-A3C6-FED66F6A650F

Q27933952-067E616D-08D1-4AC9-845F-38E15AA29503

Q27933952-0C9B927B-B90F-4697-AA34-1C26F57F494D

Q27933952-183B5566-8F92-4EF1-BC82-173A988B1373

Q27933952-1D2F49A0-2B51-4D7C-AC59-34BE0EF4CCCD

Q27933952-21478CC2-3E30-444F-B3CB-4D2A4AA5FD38

Q27933952-2F80E53A-1D88-4944-BA75-B54F085CAAAD

Q27933952-364EF968-5516-475A-9ED3-86153122DBA0

Q27933952-36CAB0A9-3305-4227-B66F-15A3F50C2C17

Q27933952-3803501C-47C8-4F56-B51C-B9A046B900D1

P304

Q27933952-D25A05F2-20DE-42FC-8BE2-CFFA13DDDAF9

P31

Q27933952-FBD745DE-2E55-4D38-AF6D-745B10844CEE

P3181

Q27933952-CC1BB250-4BC1-4604-B090-0F2CCD1C6967

P356

Q27933952-49D15239-937E-4258-ACB2-DEEC668C3C49

P407

Q27933952-23669316-6693-4E0D-AA55-2106418BA38D

P433

Q27933952-63F64C9D-312F-4E84-B40F-5773FC3D895F

P478

Q27933952-799514E0-4585-44AA-8977-B268883CE624

P577

Q27933952-1A8CAA6C-74D8-426F-959A-D60A836803C2

P698

Q27933952-799E3E92-185A-4DEF-B92A-B9AA9B84CF0D

P3181

P356

P1433

Journal of Biological Chemistry

P1476

Thio-modification of yeast cyt ...... erial sulfur transfer systems.

@en

P2093

Hideyuki Hayashi

http://www.w3.org/2001/XMLSchema#string

Masato Nakai

http://www.w3.org/2001/XMLSchema#string

Yumi Nakai

http://www.w3.org/2001/XMLSchema#string

P2860

Structural basis for lysidine formation by ATP pyrophosphatase accompanied by a lysine-specific loop and a tRNA-recognition domain

Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: identification of an acyldisulfide-linked protein--protein conjugate that is functionally analogous to the ubiquitin/E1 complex

Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis

The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins

The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins.

Nuclear localization of yeast Nfs1p is required for cell survival.

Novel methyltransferase for modified uridine residues at the wobble position of tRNA.

A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes.

Urmylation: a ubiquitin-like pathway that functions during invasive growth and budding in yeast.

Ste20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast.

P304

27469-76

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

5082612

http://www.w3.org/2001/XMLSchema#string

P356

10.1074/JBC.M804043200

http://www.w3.org/2001/XMLSchema#string

P407

P433

41

http://www.w3.org/2001/XMLSchema#string

P478

283

http://www.w3.org/2001/XMLSchema#string

P577

2008-10-10T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

18664566

http://www.w3.org/2001/XMLSchema#string