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Different subcellular localisations of TRIM22 suggest species-specific function

The B30.2/SPRY domain is present in many proteins, including various members of the tripartite motif (TRIM) protein family such as TRIM5α, which mediates innate intracellular resistance to retroviruses in several primate species. This resistance is dependent on the integrity of the B30.2 domain that...

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Detalles Bibliográficos
Autores principales: Herr, Anna-Maria, Dressel, Ralf, Walter, Lutz
Formato: Texto
Lenguaje:English
Publicado: Springer-Verlag 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3085756/
https://www.ncbi.nlm.nih.gov/pubmed/19212762
http://dx.doi.org/10.1007/s00251-009-0357-z
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author Herr, Anna-Maria
Dressel, Ralf
Walter, Lutz
author_facet Herr, Anna-Maria
Dressel, Ralf
Walter, Lutz
author_sort Herr, Anna-Maria
collection PubMed
description The B30.2/SPRY domain is present in many proteins, including various members of the tripartite motif (TRIM) protein family such as TRIM5α, which mediates innate intracellular resistance to retroviruses in several primate species. This resistance is dependent on the integrity of the B30.2 domain that evolves rapidly in primates and exhibits species-specific anti-viral activity. TRIM22 is another positively selected TRIM gene. Particularly, the B30.2 domain shows rapid evolution in the primate lineage and recently published data indicate an anti-viral function of TRIM22. We show here that human and rhesus TRIM22 localise to different subcellular compartments and that this difference can be assigned to the positively selected B30.2 domain. Moreover, we could demonstrate that amino acid changes in two variable loops (VL1 and VL3) are responsible for the different subcellular localisations.
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spelling pubmed-30857562011-06-06 Different subcellular localisations of TRIM22 suggest species-specific function Herr, Anna-Maria Dressel, Ralf Walter, Lutz Immunogenetics Original Paper The B30.2/SPRY domain is present in many proteins, including various members of the tripartite motif (TRIM) protein family such as TRIM5α, which mediates innate intracellular resistance to retroviruses in several primate species. This resistance is dependent on the integrity of the B30.2 domain that evolves rapidly in primates and exhibits species-specific anti-viral activity. TRIM22 is another positively selected TRIM gene. Particularly, the B30.2 domain shows rapid evolution in the primate lineage and recently published data indicate an anti-viral function of TRIM22. We show here that human and rhesus TRIM22 localise to different subcellular compartments and that this difference can be assigned to the positively selected B30.2 domain. Moreover, we could demonstrate that amino acid changes in two variable loops (VL1 and VL3) are responsible for the different subcellular localisations. Springer-Verlag 2009-02-11 2009-04 /pmc/articles/PMC3085756/ /pubmed/19212762 http://dx.doi.org/10.1007/s00251-009-0357-z Text en © Springer-Verlag 2009
spellingShingle Original Paper
Herr, Anna-Maria
Dressel, Ralf
Walter, Lutz
Different subcellular localisations of TRIM22 suggest species-specific function
title Different subcellular localisations of TRIM22 suggest species-specific function
title_full Different subcellular localisations of TRIM22 suggest species-specific function
title_fullStr Different subcellular localisations of TRIM22 suggest species-specific function
title_full_unstemmed Different subcellular localisations of TRIM22 suggest species-specific function
title_short Different subcellular localisations of TRIM22 suggest species-specific function
title_sort different subcellular localisations of trim22 suggest species-specific function
topic Original Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3085756/
https://www.ncbi.nlm.nih.gov/pubmed/19212762
http://dx.doi.org/10.1007/s00251-009-0357-z
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