(1)H, (13)C, and (15)N chemical shift assignments of ZCCHC9

ZCCHC9 is a human nuclear protein with sequence homology to yeast Air1p/Air2p proteins which are RNA-binding subunits of the Trf4/Air2/Mtr4 polyadenylation (TRAMP) complex involved in nuclear RNA quality control and degradation in yeast. The ZCCHC9 protein contains four retroviral-type zinc knuckle...

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Detalles Bibliográficos
Autores principales: Sanudo, Maria, Jacko, Martin, Rammelt, Christiane, Vanacova, Stepanka, Stefl, Richard
Formato: Texto
Lenguaje:English
Publicado: Springer Netherlands 2010
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3049224/
https://www.ncbi.nlm.nih.gov/pubmed/20711761
http://dx.doi.org/10.1007/s12104-010-9257-2
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author Sanudo, Maria
Jacko, Martin
Rammelt, Christiane
Vanacova, Stepanka
Stefl, Richard
author_facet Sanudo, Maria
Jacko, Martin
Rammelt, Christiane
Vanacova, Stepanka
Stefl, Richard
author_sort Sanudo, Maria
collection PubMed
description ZCCHC9 is a human nuclear protein with sequence homology to yeast Air1p/Air2p proteins which are RNA-binding subunits of the Trf4/Air2/Mtr4 polyadenylation (TRAMP) complex involved in nuclear RNA quality control and degradation in yeast. The ZCCHC9 protein contains four retroviral-type zinc knuckle motifs. Here, we report the NMR spectral assignment of the zinc knuckle region of ZCCHC9. These data will allow performing NMR structural and RNA-binding studies of ZCCHC9 with the aim to investigate its role in the RNA quality control in human.
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spelling pubmed-30492242011-04-05 (1)H, (13)C, and (15)N chemical shift assignments of ZCCHC9 Sanudo, Maria Jacko, Martin Rammelt, Christiane Vanacova, Stepanka Stefl, Richard Biomol NMR Assign Article ZCCHC9 is a human nuclear protein with sequence homology to yeast Air1p/Air2p proteins which are RNA-binding subunits of the Trf4/Air2/Mtr4 polyadenylation (TRAMP) complex involved in nuclear RNA quality control and degradation in yeast. The ZCCHC9 protein contains four retroviral-type zinc knuckle motifs. Here, we report the NMR spectral assignment of the zinc knuckle region of ZCCHC9. These data will allow performing NMR structural and RNA-binding studies of ZCCHC9 with the aim to investigate its role in the RNA quality control in human. Springer Netherlands 2010-08-14 2011 /pmc/articles/PMC3049224/ /pubmed/20711761 http://dx.doi.org/10.1007/s12104-010-9257-2 Text en © The Author(s) 2010 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Article
Sanudo, Maria
Jacko, Martin
Rammelt, Christiane
Vanacova, Stepanka
Stefl, Richard
(1)H, (13)C, and (15)N chemical shift assignments of ZCCHC9
title (1)H, (13)C, and (15)N chemical shift assignments of ZCCHC9
title_full (1)H, (13)C, and (15)N chemical shift assignments of ZCCHC9
title_fullStr (1)H, (13)C, and (15)N chemical shift assignments of ZCCHC9
title_full_unstemmed (1)H, (13)C, and (15)N chemical shift assignments of ZCCHC9
title_short (1)H, (13)C, and (15)N chemical shift assignments of ZCCHC9
title_sort (1)h, (13)c, and (15)n chemical shift assignments of zcchc9
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3049224/
https://www.ncbi.nlm.nih.gov/pubmed/20711761
http://dx.doi.org/10.1007/s12104-010-9257-2
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