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NMR solution structures of Runella slithyformis RNA 2'-phosphotransferase Tpt1 provide insights into NAD+ binding and specificity.
Alphonse S, Banerjee A, Dantuluri S, Shuman S, Ghose R. Alphonse S, et al. Nucleic Acids Res. 2021 Sep 27;49(17):9607-9624. doi: 10.1093/nar/gkab241. Nucleic Acids Res. 2021. PMID: 33880546 Free PMC article.
Here, we report NMR structures of the Tpt1 ortholog from the bacterium Runella slithyformis (RslTpt1), as apoenzyme and bound to NAD+. RslTpt1 consists of N- and C-terminal lobes with substantial inter-lobe dynamics in the free and NAD+-bound states. ...
Here, we report NMR structures of the Tpt1 ortholog from the bacterium Runella slithyformis (RslTpt1), as apoenzyme and bound …
Structural insights into the substrate specificity and activity of a novel mannose 2-epimerase from Runella slithyformis.
Wang H, Sun X, Saburi W, Hashiguchi S, Yu J, Ose T, Mori H, Yao M. Wang H, et al. Acta Crystallogr D Struct Biol. 2023 Jul 1;79(Pt 7):585-595. doi: 10.1107/S205979832300390X. Epub 2023 Jun 14. Acta Crystallogr D Struct Biol. 2023. PMID: 37314406
However, the substrate-recognition and catalytic mechanism of ME remains unknown. In this study, structures of Runella slithyformis ME (RsME) and its D254A mutant [RsME(D254A)] were determined in their apo forms and as intermediate-analog complexes [RsME-D-glucitol …
However, the substrate-recognition and catalytic mechanism of ME remains unknown. In this study, structures of Runella slithyformi
Two-step mechanism and step-arrest mutants of Runella slithyformis NAD(+)-dependent tRNA 2'-phosphotransferase Tpt1.
Munir A, Abdullahu L, Damha MJ, Shuman S. Munir A, et al. RNA. 2018 Sep;24(9):1144-1157. doi: 10.1261/rna.067165.118. Epub 2018 Jun 8. RNA. 2018. PMID: 29884622 Free PMC article.
Here we characterize the RslTpt1 protein from the bacterium Runella slithyformis, in which Tpt1 is encoded within a putative RNA repair gene cluster. ...
Here we characterize the RslTpt1 protein from the bacterium Runella slithyformis, in which Tpt1 is encoded within a putative R …
Complete genome sequence of the aquatic bacterium Runella slithyformis type strain (LSU 4(T)).
Copeland A, Zhang X, Misra M, Lapidus A, Nolan M, Lucas S, Deshpande S, Cheng JF, Tapia R, Goodwin LA, Pitluck S, Liolios K, Pagani I, Ivanova N, Mikhailova N, Pati A, Chen A, Palaniappan K, Land M, Hauser L, Pan C, Jeffries CD, Detter JC, Brambilla EM, Rohde M, Djao OD, Göker M, Sikorski J, Tindall BJ, Woyke T, Bristow J, Eisen JA, Markowitz V, Hugenholtz P, Kyrpides NC, Klenk HP, Mavromatis K. Copeland A, et al. Stand Genomic Sci. 2012 May 25;6(2):145-54. doi: 10.4056/sigs.2475579. Epub 2012 May 4. Stand Genomic Sci. 2012. PMID: 22768358 Free PMC article.
Runella slithyformis Larkin and Williams 1978 is the type species of the genus Runella, which belongs to the Cytophagaceae, a family that was only recently classified to the order Cytophagales in the class Cytophagia. ...
Runella slithyformis Larkin and Williams 1978 is the type species of the genus Runella, which belongs to the Cytophagaceae, a
Runella aurantiaca sp. nov., isolated from sludge of a manganese mine.
Yang X, Zhou Z, Liao S, Wang G. Yang X, et al. Int J Syst Evol Microbiol. 2020 Apr;70(4):2174-2177. doi: 10.1099/ijsem.0.003435. Epub 2019 May 22. Int J Syst Evol Microbiol. 2020. PMID: 31120415
Analysis of the 16S rRNA gene sequence revealed that strain YX9(T) formed the same branch within the members of the genus Runella and showed high relatedness to Runella slithyformis DSM 19594(T) (98.1 %), Runella palustris HMF3829(T) (96.0 %) and Runella zeae NS12(T …
Analysis of the 16S rRNA gene sequence revealed that strain YX9(T) formed the same branch within the members of the genus Runella and showed …
Runella palustris sp. nov., isolated from wetland freshwater.
Kim H, Kang H, Joung Y, Joh K. Kim H, et al. Int J Syst Evol Microbiol. 2017 Apr;67(3):676-680. doi: 10.1099/ijsem.0.001692. Epub 2017 Apr 3. Int J Syst Evol Microbiol. 2017. PMID: 27902287
Strain HMF3829T was closely related to Runella slithyformis DSM 19594T (95.2 % 16S rRNA gene sequence similarity), Runellalimosa DSM 17973T (94.9 %), Runellazeae NS12T (94.2 %) and Runella defluvii EMB13T (94.0 %). ...
Strain HMF3829T was closely related to Runella slithyformis DSM 19594T (95.2 % 16S rRNA gene sequence similarity), Runellalimo …
Runella soli sp. nov., isolated from garden soil.
Chhetri G, Kim J, Kim I, Kim MK, Seo T. Chhetri G, et al. Antonie Van Leeuwenhoek. 2019 Aug;112(8):1245-1252. doi: 10.1007/s10482-019-01257-9. Epub 2019 Mar 26. Antonie Van Leeuwenhoek. 2019. PMID: 30915611
The 16S rRNA gene sequence analysis showed that strain 15J11-1(T) is phylogenetically related to Runella slithyformis DSM 19594(T) and Runella palustris HMF3829(T) (96.9% and 95.4% sequence similarity, respectively). ...
The 16S rRNA gene sequence analysis showed that strain 15J11-1(T) is phylogenetically related to Runella slithyformis DSM 1959 …
Runella salmonicolor sp. nov. and Dyella lutea sp. nov., isolated from paddy field soil.
Park S, Kim I, Chhetri G, So Y, Jung Y, Woo H, Seo T. Park S, et al. Int J Syst Evol Microbiol. 2023 Jun;73(6). doi: 10.1099/ijsem.0.005938. Int J Syst Evol Microbiol. 2023. PMID: 37358382
S5(T) exhibited 99.22, 98.10 and 97.68 % similarity to Runella rosea HYN0085(T), Runella aurantiaca YX9(T) and Runella slithyformis DSM 19594(T), respectively. S5(T) grew at 15-40 C (optimum, 25 C), at pH 6.5-12.0 (optimum, pH 9.5) and in the presence of 0-0.5 % (w/ …
S5(T) exhibited 99.22, 98.10 and 97.68 % similarity to Runella rosea HYN0085(T), Runella aurantiaca YX9(T) and Runella slithyformi
Structure-Function Analysis of the Phosphoesterase Component of the Nucleic Acid End-Healing Enzyme Runella slithyformis HD-Pnk.
Munir A, Shuman S. Munir A, et al. J Bacteriol. 2019 Jul 24;201(16):e00292-19. doi: 10.1128/JB.00292-19. Print 2019 Aug 15. J Bacteriol. 2019. PMID: 31160396 Free PMC article.
Runella slithyformis HD-Pnk is the prototype of a family of dual 5' and 3' nucleic acid end-healing enzymes that phosphorylate 5'-OH termini and dephosphorylate 2',3'-cyclic-PO(4), 3'-PO(4), and 2'-PO(4) ends. ...This study interrogates, biochemically and via mutage
Runella slithyformis HD-Pnk is the prototype of a family of dual 5' and 3' nucleic acid end-healing enzymes that phosphorylate
Characterization of Runella slithyformis HD-Pnk, a Bifunctional DNA/RNA End-Healing Enzyme Composed of an N-Terminal 2',3'-Phosphoesterase HD Domain and a C-Terminal 5'-OH Polynucleotide Kinase Domain.
Munir A, Shuman S. Munir A, et al. J Bacteriol. 2017 Jan 12;199(3):e00739-16. doi: 10.1128/JB.00739-16. Print 2017 Feb 1. J Bacteriol. 2017. PMID: 27895092 Free PMC article.
End-healing and sealing enzymes are present in diverse bacterial taxa, often organized as modular units within a single multifunctional polypeptide or as subunits of a repair complex. Here we identify and characterize Runella slithyformis HD-Pnk as a novel bifunctio …
End-healing and sealing enzymes are present in diverse bacterial taxa, often organized as modular units within a single multifunctional poly …
18 results