The pseudouridine synthase RluD is required for normal ribosome assembly and function in Escherichia coli. - Wikidata - wikimedia - TriplyDB

The pseudouridine synthase RluD is required for normal ribosome assembly and function in Escherichia coli.

The pseudouridine synthase RluD is required for normal ribosome assembly and function in Escherichia coli.

http://www.wikidata.org/entity/Q42010185

about

Identification and characterization of RsmE, the founding member of a new RNA base methyltransferase family How U38, 39, and 40 of Many tRNAs Become the Targets for Pseudouridylation by TruA Structural and Functional Characterization of Rv2966c Protein Reveals an RsmD-like Methyltransferase from Mycobacterium tuberculosis and the Role of Its N-terminal Domain in Target Recognition Small RNAs endow a transcriptional activator with essential repressor functions for single-tier control of a global stress regulon Ribosome biogenesis and the translation process in Escherichia coli Conserved loop sequence of helix 69 in Escherichia coli 23 S rRNA is involved in A-site tRNA binding and translational fidelity.The E. coli RhlE RNA helicase regulates the function of related RNA helicases during ribosome assembly Genetic interaction screens with ordered overexpression and deletion clone sets implicate the Escherichia coli GTPase YjeQ in late ribosome biogenesis.Environmental adaptation: genomic analysis of the piezotolerant and psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans WP3 Binding of aminoglycoside antibiotics to helix 69 of 23S rRNA Base methylations in the double-stranded RNA by a fused methyltransferase bearing unwinding activity Inactivation of the RluD pseudouridine synthase has minimal effects on growth and ribosome function in wild-type Escherichia coli and Salmonella enterica.Deletion of the RluD pseudouridine synthase promotes SsrA peptide tagging of ribosomal protein S7 Substrate specificity of the pseudouridine synthase RluD in Escherichia coli.Pseudouridylation of helix 69 of 23S rRNA is necessary for an effective translation termination.An indigenous posttranscriptional modification in the ribosomal peptidyl transferase center confers resistance to an array of protein synthesis inhibitors.The Escherichia coli GTPase CgtAE is involved in late steps of large ribosome assembly.High-resolution structure of the Escherichia coli ribosome.Identification of novel Escherichia coli ribosome-associated proteins using isobaric tags and multidimensional protein identification techniques RluD, a highly conserved pseudouridine synthase, modifies 50S subunits more specifically and efficiently than free 23S rRNA.Pseudouridine: still mysterious, but never a fake (uridine)!Francisella tularensis live vaccine strain folate metabolism and pseudouridine synthase gene mutants modulate macrophage caspase-1 activation.The weird and wonderful world of bacterial ribosome regulation.Expanding the nucleotide repertoire of the ribosome with post-transcriptional modifications.Characterization of chromosomal regions conserved in Yersinia pseudotuberculosis and lost by Yersinia pestis Evaluating the reproducibility of quantifying modified nucleosides from ribonucleic acids by LC-UV-MS.Structural Insights into ribosome recycling factor interactions with the 70S ribosome.Identification and characterization of growth suppressors of Escherichia coli strains lacking phosphorolytic ribonucleases.Quantitative analysis of rRNA modifications using stable isotope labeling and mass spectrometry.Suppression of a cold-sensitive mutation in ribosomal protein S5 reveals a role for RimJ in ribosome biogenesis.Identification of the methyltransferase targeting C2499 in Deinococcus radiodurans 23S ribosomal RNA.Comparison of solution conformations and stabilities of modified helix 69 rRNA analogs from bacteria and human The last rRNA methyltransferase of E. coli revealed: the yhiR gene encodes adenine-N6 methyltransferase specific for modification of A2030 of 23S ribosomal RNA.Random pseuoduridylation in vivo reveals critical region of Escherichia coli 23S rRNA for ribosome assembly How much can we learn about the function of bacterial rRNA modification by mining large-scale experimental datasets?Specificity and kinetics of 23S rRNA modification enzymes RlmH and RluD.Functional defects in transfer RNAs lead to the accumulation of ribosomal RNA precursors.Functional analysis of the GTPases EngA and YhbZ encoded by Salmonella typhimurium.Mutations in SUPPRESSOR OF VARIEGATION1, a factor required for normal chloroplast translation, suppress var2-mediated leaf variegation in Arabidopsis.

P2860

Q24541405-4FE54ABF-625A-4801-9F09-7C7B6F42FB53 Q27644630-9F5A1DF5-B2F8-4F4E-B541-AB6553042790 Q27667462-A684E265-3C45-49C3-8806-84A64F458343 Q28243536-27AD70E8-1837-467A-9B6B-3DB0737A8AD2 Q28246227-2A032C5C-497D-4384-8EEE-D7B3C5E64DBE Q33240227-F152FF03-4AB3-4765-87CE-0A1E632835AD Q33310573-A77AFA62-19B9-473B-917B-4CCFB29D04C7 Q33316638-6FBC03CB-DD53-4E55-A447-40EBE82B0A9E Q33327361-66C40FFC-AC03-42CA-8EB7-2DBE77F0C63B Q33871203-F9A191EF-D317-4110-AD76-30F660F867A4 Q34243886-702BCD29-69C1-4703-B74F-35797188D26F Q34484867-786E5B0F-A688-49BD-A4DF-E1A891FCCB64 Q34543998-E604D05B-F819-4E28-B0E6-7BC83724CBBD Q34701152-00B74479-6F38-4E2E-8E81-10CAA330F94A Q34717123-8758EE9F-9502-4CE0-A2B0-27A8D08FD15B Q34786545-5F1C66D9-5E28-4CA8-AE8A-31396604B0B8 Q35075672-257E3CC8-D7C9-4D75-933F-3BCE2A0EE570 Q35598643-C9DB0927-E569-414B-B245-21DD227E1191 Q35759723-2B807E7C-6BA6-4674-BC16-884764F16B54 Q36088318-F441C9FD-8820-49E7-A8AE-41A10A0BF286 Q36190987-FAACD391-E0C2-42E6-8C9D-E6ED8C8D8160 Q36506062-2EF175D9-B39C-4104-A55B-3458571F1D8E Q36846903-F8603FA1-C571-41D6-9F73-3B2CF32AB23A Q36874021-42FD2C08-D603-4509-A319-B18704CD4A45 Q36898493-D2F302B9-DE0D-4FCC-8232-607935B78774 Q37091464-93E5F0CB-7E72-4E2C-8494-B6A6266D169A Q37266828-CB45D31A-EF4A-4BAD-BF12-19665E6488C9 Q37333283-CA7AEBD2-092D-40BB-A864-04D9FA927081 Q38732764-00D362D4-3EE3-4B8A-8CE7-AEE654CDB7AA Q39597324-E2AD158F-AC75-4AAB-9C55-D7EBFF18B956 Q40293449-BD28A499-545C-4786-BC0B-7E8E5F31E3ED Q40763369-CA0C80DE-CF18-4E9F-B353-B288CEC56DF6 Q41768024-B6977245-C359-4842-9824-3AFB07812DD1 Q41865855-BDA7EB54-B02D-44F5-9BC3-9157A53F79DC Q41873656-E7C2B097-05C1-4DCC-AEAC-2DC018D358E3 Q42064661-68631138-4E15-4A65-9B59-D0C2963E5D5C Q42908301-F38B5AED-9169-4C7A-AB79-469DAED05272 Q42971016-098CE6A3-025F-4D04-88B5-75B7F9D2C339 Q46503233-307732FB-16C1-49EA-98F1-530FF2A65AB9

P2860

The pseudouridine synthase RluD is required for normal ribosome assembly and function in Escherichia coli.

http://www.wikidata.org/entity/Q42010185

description

2005 nî lūn-bûn

@nan

2005年の論文

@ja

2005年学术文章

@wuu

2005年学术文章

@zh-cn

2005年学术文章

@zh-hans

2005年学术文章

@zh-my

2005年学术文章

@zh-sg

2005年學術文章

@yue

2005年學術文章

@zh

2005年學術文章

@zh-hant

name

The pseudouridine synthase Rlu ...... function in Escherichia coli.

@en

The pseudouridine synthase Rlu ...... function in Escherichia coli.

@nl

type

label

The pseudouridine synthase Rlu ...... function in Escherichia coli.

@en

The pseudouridine synthase Rlu ...... function in Escherichia coli.

@nl

prefLabel

The pseudouridine synthase Rlu ...... function in Escherichia coli.

@en

The pseudouridine synthase Rlu ...... function in Escherichia coli.

@nl

P1433

Q42010185-BEB244B2-3587-4B75-9FF6-B0881518C4E3

P1476

Q42010185-FF69CE95-80C3-475F-A7A1-94A426410D97

P2093

Q42010185-178B1E05-E4FF-40AF-8851-1DA0AC142425

Q42010185-1A6501D1-C617-4673-9809-EC53E9FDF93D

Q42010185-A2E69836-E48E-4556-B686-ADC949FC3EE5

P2860

Q42010185-007BC942-AFA3-4311-9EAB-819736902AC9

Q42010185-0744C6F9-961D-48E7-92C7-3B5DF925993E

Q42010185-0B150767-CC0A-4720-BCB3-34C5862C0331

Q42010185-2B4BAB99-79A9-4102-B7B1-AFC348C757A0

Q42010185-2D894C58-5593-4893-A7CA-35D699026E1C

Q42010185-304E7E67-2B7E-42B2-A04B-E6C912A3C8CB

Q42010185-3B036B18-348F-4008-BD6E-79300A346E13

Q42010185-3B48995D-62B1-4030-A3FE-A6B544008753

Q42010185-44179A8D-E528-46F9-AF60-E4FCEC88FF00

Q42010185-55CFA7D3-5DDB-4101-9619-76FEF3E3E593

P304

Q42010185-FB748767-5153-441E-95D5-3CD60089B8A0

P31

Q42010185-6CC67A82-8420-4603-8734-725074597653

P356

Q42010185-9FD7600B-CE92-45ED-8EE6-BF88B816C652

P407

Q42010185-783A3F74-BD3E-413D-BEFD-D1B516D417C1

P433

Q42010185-9C280942-B6AF-407B-9F07-86EA10B10CD0

P478

Q42010185-AA360BDE-D370-4CFA-B447-0365DDF1F5DC

P577

Q42010185-C0744449-7934-49B6-97E1-05D70D411970

P5875

Q42010185-F831C37B-016B-4FC0-9808-0E6D4B253E48

P698

Q42010185-D22AD34B-7A2C-4A0A-9E1B-30B5BBC8611C

P921

Q42010185-8A34C66F-03F9-4965-B835-A541C7E65374

P932

Q42010185-7A3C471D-C718-4642-A041-D17FDCF6D57D

P356

P1433

P1476

The pseudouridine synthase Rlu ...... function in Escherichia coli.

@en

P2093

James Ofengand

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

Murray P Deutscher

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

Nancy S Gutgsell

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

P2860

Ribosomal Crystallography: Initiation, Peptide Bond Formation, and Amino Acid Polymerization are Hampered by Antibiotics

Visualization of ribosome-recycling factor on the Escherichia coli 70S ribosome: functional implications

The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I

Crystal structure of the ribosome at 5.5 A resolution

Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression

Crystal structure of the catalytic domain of RluD, the only rRNA pseudouridine synthase required for normal growth of Escherichia coli

One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products

Pseudouridylation at position 32 of mitochondrial and cytoplasmic tRNAs requires two distinct enzymes in Saccharomyces cerevisiae.

A second function for pseudouridine synthases: A point mutant of RluD unable to form pseudouridines 1911, 1915, and 1917 in Escherichia coli 23S ribosomal RNA restores normal growth to an RluD-minus strain.

Identification and site of action of the remaining four putative pseudouridine synthases in Escherichia coli

P304

1141-1152

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

P31

scholarly article

P356

10.1261/RNA.2550105

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

P407

P433

7

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

P478

11

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

P577

2005-05-31T00:00:00Z

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

P5875

7814385

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

P698

15928344

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

P921

Escherichia coli

P932

1370798

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