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DAYSLEEPER: a nuclear and vesicular-localized protein that is expressed in proliferating tissues
BACKGROUND: DAYSLEEPER is a domesticated transposase that is essential for development in Arabidopsis thaliana [Nature, 436:282–284, 2005]. It is derived from a hAT-superfamily transposon and contains many of the features found in the coding sequence of these elements [Nature, 436:282–284, 2005, Gen...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4029315/ https://www.ncbi.nlm.nih.gov/pubmed/24330683 http://dx.doi.org/10.1186/1471-2229-13-211 |
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author | Knip, Marijn Hiemstra, Steven Sietsma, Afke Castelein, Marina de Pater, Sylvia Hooykaas, Paul |
author_facet | Knip, Marijn Hiemstra, Steven Sietsma, Afke Castelein, Marina de Pater, Sylvia Hooykaas, Paul |
author_sort | Knip, Marijn |
collection | PubMed |
description | BACKGROUND: DAYSLEEPER is a domesticated transposase that is essential for development in Arabidopsis thaliana [Nature, 436:282–284, 2005]. It is derived from a hAT-superfamily transposon and contains many of the features found in the coding sequence of these elements [Nature, 436:282–284, 2005, Genetics, 158:949–957, 2001]. This work sheds light on the expression of this gene and localization of its product in protoplasts and in planta. Using deletion constructs, important domains in the protein were identified. RESULTS: DAYSLEEPER is predominantly expressed in meristems, developing flowers and siliques. The protein is mainly localized in the nucleus, but can also be seen in discrete foci in the cytoplasm. Using several vesicular markers, we found that these foci belong to vesicular structures of the trans-golgi network, multivesicular bodies (MVB’s) and late endosomes. The central region as well as both the N- and the C-terminus are essential to DAYSLEEPER function, since versions of DAYSLEEPER deleted for these regions are not able to complement the daysleeper phenotype. Like hAT-transposases, we show that DAYSLEEPER has a functionally conserved dimerization domain [J Biol Chem, 282:7563–7575, 2007]. CONCLUSIONS: DAYSLEEPER has retained the global structure of hAT transposases and it seems that most of these conserved features are essential to DAYSLEEPER’s cellular function. Although structurally similar, DAYSLEEPER seems to have broadened its range of action beyond the nucleus in comparison to transposases. |
format | Online Article Text |
id | pubmed-4029315 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-40293152014-05-22 DAYSLEEPER: a nuclear and vesicular-localized protein that is expressed in proliferating tissues Knip, Marijn Hiemstra, Steven Sietsma, Afke Castelein, Marina de Pater, Sylvia Hooykaas, Paul BMC Plant Biol Research Article BACKGROUND: DAYSLEEPER is a domesticated transposase that is essential for development in Arabidopsis thaliana [Nature, 436:282–284, 2005]. It is derived from a hAT-superfamily transposon and contains many of the features found in the coding sequence of these elements [Nature, 436:282–284, 2005, Genetics, 158:949–957, 2001]. This work sheds light on the expression of this gene and localization of its product in protoplasts and in planta. Using deletion constructs, important domains in the protein were identified. RESULTS: DAYSLEEPER is predominantly expressed in meristems, developing flowers and siliques. The protein is mainly localized in the nucleus, but can also be seen in discrete foci in the cytoplasm. Using several vesicular markers, we found that these foci belong to vesicular structures of the trans-golgi network, multivesicular bodies (MVB’s) and late endosomes. The central region as well as both the N- and the C-terminus are essential to DAYSLEEPER function, since versions of DAYSLEEPER deleted for these regions are not able to complement the daysleeper phenotype. Like hAT-transposases, we show that DAYSLEEPER has a functionally conserved dimerization domain [J Biol Chem, 282:7563–7575, 2007]. CONCLUSIONS: DAYSLEEPER has retained the global structure of hAT transposases and it seems that most of these conserved features are essential to DAYSLEEPER’s cellular function. Although structurally similar, DAYSLEEPER seems to have broadened its range of action beyond the nucleus in comparison to transposases. BioMed Central 2013-12-12 /pmc/articles/PMC4029315/ /pubmed/24330683 http://dx.doi.org/10.1186/1471-2229-13-211 Text en Copyright © 2013 Knip et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Knip, Marijn Hiemstra, Steven Sietsma, Afke Castelein, Marina de Pater, Sylvia Hooykaas, Paul DAYSLEEPER: a nuclear and vesicular-localized protein that is expressed in proliferating tissues |
title | DAYSLEEPER: a nuclear and vesicular-localized protein that is expressed in proliferating tissues |
title_full | DAYSLEEPER: a nuclear and vesicular-localized protein that is expressed in proliferating tissues |
title_fullStr | DAYSLEEPER: a nuclear and vesicular-localized protein that is expressed in proliferating tissues |
title_full_unstemmed | DAYSLEEPER: a nuclear and vesicular-localized protein that is expressed in proliferating tissues |
title_short | DAYSLEEPER: a nuclear and vesicular-localized protein that is expressed in proliferating tissues |
title_sort | daysleeper: a nuclear and vesicular-localized protein that is expressed in proliferating tissues |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4029315/ https://www.ncbi.nlm.nih.gov/pubmed/24330683 http://dx.doi.org/10.1186/1471-2229-13-211 |
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