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AP-APSE dpol intein: A novel family A DNA polymerase intein domain

Inteins are “protein introns” that remove themselves from their host proteins through an autocatalytic protein-splicing. After their discovery, inteins have been quickly identified in organisms from all three kingdoms of life - eucarya, bacteria and archaea, but their distribution is sporadic. Here...

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Detalles Bibliográficos
Autores principales: Rajarajan, Senguttuvan, Ibrahim, Kalibulla Syed, Pandian, Shunmugiah Karutha
Formato: Texto
Lenguaje:English
Publicado: Biomedical Informatics 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3092948/
https://www.ncbi.nlm.nih.gov/pubmed/21572881
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author Rajarajan, Senguttuvan
Ibrahim, Kalibulla Syed
Pandian, Shunmugiah Karutha
author_facet Rajarajan, Senguttuvan
Ibrahim, Kalibulla Syed
Pandian, Shunmugiah Karutha
author_sort Rajarajan, Senguttuvan
collection PubMed
description Inteins are “protein introns” that remove themselves from their host proteins through an autocatalytic protein-splicing. After their discovery, inteins have been quickly identified in organisms from all three kingdoms of life - eucarya, bacteria and archaea, but their distribution is sporadic. Here we report the identification and bioinformatics characterization of intein in DNA polymerase A gene of bacteriophage APSE (Acyrthosiphon pisum Secondary Endosymbiont bacteriophage) infecting the Aphid secondary endosymbionts of eukaryotic insects such as Acyrthosiphon pisum, Uroleucon rudbeckiae. The insertion site of intein within APSE family A DNA polymerase extein was identified to be dpola. Hence we propose this as a unique intein of family A DNA polymerase (dpola insertion site) and only reported intein in podoviridae family.
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spelling pubmed-30929482011-05-13 AP-APSE dpol intein: A novel family A DNA polymerase intein domain Rajarajan, Senguttuvan Ibrahim, Kalibulla Syed Pandian, Shunmugiah Karutha Bioinformation Hypothesis Inteins are “protein introns” that remove themselves from their host proteins through an autocatalytic protein-splicing. After their discovery, inteins have been quickly identified in organisms from all three kingdoms of life - eucarya, bacteria and archaea, but their distribution is sporadic. Here we report the identification and bioinformatics characterization of intein in DNA polymerase A gene of bacteriophage APSE (Acyrthosiphon pisum Secondary Endosymbiont bacteriophage) infecting the Aphid secondary endosymbionts of eukaryotic insects such as Acyrthosiphon pisum, Uroleucon rudbeckiae. The insertion site of intein within APSE family A DNA polymerase extein was identified to be dpola. Hence we propose this as a unique intein of family A DNA polymerase (dpola insertion site) and only reported intein in podoviridae family. Biomedical Informatics 2011-05-07 /pmc/articles/PMC3092948/ /pubmed/21572881 Text en © 2011 Biomedical Informatics This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Hypothesis
Rajarajan, Senguttuvan
Ibrahim, Kalibulla Syed
Pandian, Shunmugiah Karutha
AP-APSE dpol intein: A novel family A DNA polymerase intein domain
title AP-APSE dpol intein: A novel family A DNA polymerase intein domain
title_full AP-APSE dpol intein: A novel family A DNA polymerase intein domain
title_fullStr AP-APSE dpol intein: A novel family A DNA polymerase intein domain
title_full_unstemmed AP-APSE dpol intein: A novel family A DNA polymerase intein domain
title_short AP-APSE dpol intein: A novel family A DNA polymerase intein domain
title_sort ap-apse dpol intein: a novel family a dna polymerase intein domain
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3092948/
https://www.ncbi.nlm.nih.gov/pubmed/21572881
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