Phosphorylation at serines 216 and 221 is important for Drosophila HeT-A Gag protein stability.

Telomeres from Drosophila appear to be very different from those of other organisms - in size and the mechanism of their maintenance. In the absence of the enzyme telomerase, Drosophila telomeres are maintained by retrotransposition of three elements, HeT-A, TART, and TAHRE, but details of their tra...

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Autores principales:	Sukhdev S Brar, Robert M Petrovich, Jason G Williams, James M Mason
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/47a153c2082548879f93703630c45386
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spelling	oai:doaj.org-article:47a153c2082548879f93703630c453862021-11-18T08:54:39ZPhosphorylation at serines 216 and 221 is important for Drosophila HeT-A Gag protein stability.1932-620310.1371/journal.pone.0075381https://doaj.org/article/47a153c2082548879f93703630c453862013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24058682/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Telomeres from Drosophila appear to be very different from those of other organisms - in size and the mechanism of their maintenance. In the absence of the enzyme telomerase, Drosophila telomeres are maintained by retrotransposition of three elements, HeT-A, TART, and TAHRE, but details of their transposition mechanisms are not known. Here we characterized some biochemical characteristics of the HeT-A Gag protein encoded by the HeT-A element to understand this mechanism. The HeT-A Gag protein when overexpressed in S2 cells was localized to the nucleus but was resistant to high salt, detergents and nuclease extraction treatments. Analysis of the HeT-A Gag protein by tandem mass spectrophotometry revealed that serines 216 and 221 are phosphorylated. Substituting these serines with alanine or aspartic acid by site-directed mutagenesis did not result in any changes in HeT-A Gag translocation across the nucleus, suggesting that phosphorylation of these sites is not associated with HeT-A Gag translocation, but time course experiments showed that these phosphorylation sites are important for Gag-protein stability.Sukhdev S BrarRobert M PetrovichJason G WilliamsJames M MasonPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 9, p e75381 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sukhdev S Brar Robert M Petrovich Jason G Williams James M Mason Phosphorylation at serines 216 and 221 is important for Drosophila HeT-A Gag protein stability.
description	Telomeres from Drosophila appear to be very different from those of other organisms - in size and the mechanism of their maintenance. In the absence of the enzyme telomerase, Drosophila telomeres are maintained by retrotransposition of three elements, HeT-A, TART, and TAHRE, but details of their transposition mechanisms are not known. Here we characterized some biochemical characteristics of the HeT-A Gag protein encoded by the HeT-A element to understand this mechanism. The HeT-A Gag protein when overexpressed in S2 cells was localized to the nucleus but was resistant to high salt, detergents and nuclease extraction treatments. Analysis of the HeT-A Gag protein by tandem mass spectrophotometry revealed that serines 216 and 221 are phosphorylated. Substituting these serines with alanine or aspartic acid by site-directed mutagenesis did not result in any changes in HeT-A Gag translocation across the nucleus, suggesting that phosphorylation of these sites is not associated with HeT-A Gag translocation, but time course experiments showed that these phosphorylation sites are important for Gag-protein stability.
format	article
author	Sukhdev S Brar Robert M Petrovich Jason G Williams James M Mason
author_facet	Sukhdev S Brar Robert M Petrovich Jason G Williams James M Mason
author_sort	Sukhdev S Brar
title	Phosphorylation at serines 216 and 221 is important for Drosophila HeT-A Gag protein stability.
title_short	Phosphorylation at serines 216 and 221 is important for Drosophila HeT-A Gag protein stability.
title_full	Phosphorylation at serines 216 and 221 is important for Drosophila HeT-A Gag protein stability.
title_fullStr	Phosphorylation at serines 216 and 221 is important for Drosophila HeT-A Gag protein stability.
title_full_unstemmed	Phosphorylation at serines 216 and 221 is important for Drosophila HeT-A Gag protein stability.
title_sort	phosphorylation at serines 216 and 221 is important for drosophila het-a gag protein stability.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/47a153c2082548879f93703630c45386
work_keys_str_mv	AT sukhdevsbrar phosphorylationatserines216and221isimportantfordrosophilahetagagproteinstability AT robertmpetrovich phosphorylationatserines216and221isimportantfordrosophilahetagagproteinstability AT jasongwilliams phosphorylationatserines216and221isimportantfordrosophilahetagagproteinstability AT jamesmmason phosphorylationatserines216and221isimportantfordrosophilahetagagproteinstability
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Phosphorylation at serines 216 and 221 is important for Drosophila HeT-A Gag protein stability.

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