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The XLR gene product defines a novel set of proteins stabilized in the nucleus by zinc ions

The major product of the XLR (X-chromosomal, lymphocyte-regulated) locus is found to be a 30-kD nuclear protein with a relatively short (t1/2 approximately equal to 2 h) half-life. Together with its stage- and tissue-specific pattern of expression, this suggests a role for this protein in the regula...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1989
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115372/
https://www.ncbi.nlm.nih.gov/pubmed/2493459
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description The major product of the XLR (X-chromosomal, lymphocyte-regulated) locus is found to be a 30-kD nuclear protein with a relatively short (t1/2 approximately equal to 2 h) half-life. Together with its stage- and tissue-specific pattern of expression, this suggests a role for this protein in the regulation of differentiation in T and B lymphocytes. Interestingly, the XLR protein almost completely leaches out of the nucleus after lysis of cells in low salt buffer, but is stabilized in that location by metal cations, particularly Zn++. This stabilization is reversible by chelating agents (o-phenanthroline, EDTA) which also release a number of other polypeptides in addition to XLR. These results suggest that XLR represents a novel class of nuclear proteins, and that cations such as zinc may play a role in the localization of these proteins in the nucleus.
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spelling pubmed-21153722008-05-01 The XLR gene product defines a novel set of proteins stabilized in the nucleus by zinc ions J Cell Biol Articles The major product of the XLR (X-chromosomal, lymphocyte-regulated) locus is found to be a 30-kD nuclear protein with a relatively short (t1/2 approximately equal to 2 h) half-life. Together with its stage- and tissue-specific pattern of expression, this suggests a role for this protein in the regulation of differentiation in T and B lymphocytes. Interestingly, the XLR protein almost completely leaches out of the nucleus after lysis of cells in low salt buffer, but is stabilized in that location by metal cations, particularly Zn++. This stabilization is reversible by chelating agents (o-phenanthroline, EDTA) which also release a number of other polypeptides in addition to XLR. These results suggest that XLR represents a novel class of nuclear proteins, and that cations such as zinc may play a role in the localization of these proteins in the nucleus. The Rockefeller University Press 1989-03-01 /pmc/articles/PMC2115372/ /pubmed/2493459 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
The XLR gene product defines a novel set of proteins stabilized in the nucleus by zinc ions
title The XLR gene product defines a novel set of proteins stabilized in the nucleus by zinc ions
title_full The XLR gene product defines a novel set of proteins stabilized in the nucleus by zinc ions
title_fullStr The XLR gene product defines a novel set of proteins stabilized in the nucleus by zinc ions
title_full_unstemmed The XLR gene product defines a novel set of proteins stabilized in the nucleus by zinc ions
title_short The XLR gene product defines a novel set of proteins stabilized in the nucleus by zinc ions
title_sort xlr gene product defines a novel set of proteins stabilized in the nucleus by zinc ions
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115372/
https://www.ncbi.nlm.nih.gov/pubmed/2493459