Pseudouridine synthase: Difference between revisions
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*'''RluE''' is responsible for synthesis of pseudouridine from uracil in position 2457 in 23S ribosomal RNA<ref>PMID:17320904</ref>.<br /> | *'''RluE''' is responsible for synthesis of pseudouridine from uracil in position 2457 in 23S ribosomal RNA<ref>PMID:17320904</ref>.<br /> | ||
*'''RluF''' is responsible for synthesis of pseudouridine from uracil in position 2604 in 23S ribosomal RNA<ref>PMID:16712869</ref>.<br /> | *'''RluF''' is responsible for synthesis of pseudouridine from uracil in position 2604 in 23S ribosomal RNA<ref>PMID:16712869</ref>.<br /> | ||
Ribosomal small subunit pseudouridine synthase'''RsuA''' is responsible for synthesis of pseudouridine from uracil in positions 516 in 16S ribosomal RNA<ref>PMID:11953756</ref>.<br /> | |||
== Structural highlights == | == Structural highlights == |
Revision as of 14:14, 12 November 2018
FunctiontRNA pseudouridine synthase (PUS) catalyzes the conversion of tRNA uridine to tRNA pseudouridine[1]. Probable tRNA pseudouridine synthase (PPUS) is a similar enzyme. PUS are active in the ribosomal large subunit Ribosomal large subunit pseudouridine synthase and in the ribosomal small subunit Ribosomal small subunit pseudouridine synthase. Ribosomal large subunit pseudouridine synthases:
Ribosomal small subunit pseudouridine synthaseRsuA is responsible for synthesis of pseudouridine from uracil in positions 516 in 16S ribosomal RNA[8]. Structural highlightsThe conversion of uridine to pseudouridine causes conformational change of PUS[9]. (1ze2). |
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3D Structures of tRNA pseudouridine synthase3D Structures of tRNA pseudouridine synthase
Updated on 12-November-2018
ReferencesReferences
- ↑ Pan H, Agarwalla S, Moustakas DT, Finer-Moore J, Stroud RM. Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit. Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12648-53. Epub 2003 Oct 17. PMID:14566049 doi:10.1073/pnas.2135585100
- ↑ Hoang C, Chen J, Vizthum CA, Kandel JM, Hamilton CS, Mueller EG, Ferre-D'Amare AR. Crystal structure of pseudouridine synthase RluA: indirect sequence readout through protein-induced RNA structure. Mol Cell. 2006 Nov 17;24(4):535-45. PMID:17188032 doi:10.1016/j.molcel.2006.09.017
- ↑ Czudnochowski N, Ashley GW, Santi DV, Alian A, Finer-Moore J, Stroud RM. The mechanism of pseudouridine synthases from a covalent complex with RNA, and alternate specificity for U2605 versus U2604 between close homologs. Nucleic Acids Res. 2013 Nov 7. PMID:24214967 doi:http://dx.doi.org/10.1093/nar/gkt1050
- ↑ Conrad J, Sun D, Englund N, Ofengand J. The rluC gene of Escherichia coli codes for a pseudouridine synthase that is solely responsible for synthesis of pseudouridine at positions 955, 2504, and 2580 in 23 S ribosomal RNA. J Biol Chem. 1998 Jul 17;273(29):18562-6. PMID:9660827
- ↑ Gutgsell NS, Deutscher MP, Ofengand J. The pseudouridine synthase RluD is required for normal ribosome assembly and function in Escherichia coli. RNA. 2005 Jul;11(7):1141-52. doi: 10.1261/rna.2550105. Epub 2005 May 31. PMID:15928344 doi:http://dx.doi.org/10.1261/rna.2550105
- ↑ Pan H, Ho JD, Stroud RM, Finer-Moore J. The crystal structure of E. coli rRNA pseudouridine synthase RluE. J Mol Biol. 2007 Apr 13;367(5):1459-70. Epub 2007 Feb 7. PMID:17320904 doi:10.1016/j.jmb.2007.01.084
- ↑ Sunita S, Zhenxing H, Swaathi J, Cygler M, Matte A, Sivaraman J. Domain organization and crystal structure of the catalytic domain of E.coli RluF, a pseudouridine synthase that acts on 23S rRNA. J Mol Biol. 2006 Jun 16;359(4):998-1009. Epub 2006 Apr 25. PMID:16712869 doi:10.1016/j.jmb.2006.04.019
- ↑ Sivaraman J, Sauve V, Larocque R, Stura EA, Schrag JD, Cygler M, Matte A. Structure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP. Nat Struct Biol. 2002 May;9(5):353-8. PMID:11953756 doi:10.1038/nsb788
- ↑ Phannachet K, Huang RH. Conformational change of pseudouridine 55 synthase upon its association with RNA substrate. Nucleic Acids Res. 2004 Feb 27;32(4):1422-9. Print 2004. PMID:14990747 doi:10.1093/nar/gkh287