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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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Formato: | Texto |
Lenguaje: | English |
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Biomedical Informatics
2011
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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. |
format | Text |
id | pubmed-3092948 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Biomedical Informatics |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT rajarajansenguttuvan apapsedpolinteinanovelfamilyadnapolymeraseinteindomain AT ibrahimkalibullasyed apapsedpolinteinanovelfamilyadnapolymeraseinteindomain AT pandianshunmugiahkarutha apapsedpolinteinanovelfamilyadnapolymeraseinteindomain |