Cargando…
Homologues of bacterial TnpB_IS605 are widespread in diverse eukaryotic transposable elements
BACKGROUND: Bacterial insertion sequences (IS) of IS200/IS605 and IS607 family often encode a transposase (TnpA) and a protein of unknown function, TnpB. RESULTS: Here we report two groups of TnpB-like proteins (Fanzor1 and Fanzor2) that are widespread in diverse eukaryotic transposable elements (TE...
Autores principales: | , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3627910/ https://www.ncbi.nlm.nih.gov/pubmed/23548000 http://dx.doi.org/10.1186/1759-8753-4-12 |
_version_ | 1782266354933432320 |
---|---|
author | Bao, Weidong Jurka, Jerzy |
author_facet | Bao, Weidong Jurka, Jerzy |
author_sort | Bao, Weidong |
collection | PubMed |
description | BACKGROUND: Bacterial insertion sequences (IS) of IS200/IS605 and IS607 family often encode a transposase (TnpA) and a protein of unknown function, TnpB. RESULTS: Here we report two groups of TnpB-like proteins (Fanzor1 and Fanzor2) that are widespread in diverse eukaryotic transposable elements (TEs), and in large double-stranded DNA (dsDNA) viruses infecting eukaryotes. Fanzor and TnpB proteins share the same conserved amino acid motif in their C-terminal half regions: D-X(125, 275)-[TS]-[TS]-X-X-[C4 zinc finger]-X(5,50)-RD, but are highly variable in their N-terminal regions. Fanzor1 proteins are frequently captured by DNA transposons from different superfamilies including Helitron, Mariner, IS4-like, Sola and MuDr. In contrast, Fanzor2 proteins appear only in some IS607-type elements. We also analyze a new Helitron2 group from the Helitron superfamily, which contains elements with hairpin structures on both ends. Non-autonomous Helitron2 elements (CRe-1, 2, 3) in the genome of green alga Chlamydomonas reinhardtii are flanked by target site duplications (TSDs) of variable length (approximately 7 to 19 bp). CONCLUSIONS: The phylogeny and distribution of the TnpB/Fanzor proteins indicate that they may be disseminated among eukaryotic species by viruses. We hypothesize that TnpB/Fanzor proteins may act as methyltransferases. |
format | Online Article Text |
id | pubmed-3627910 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-36279102013-04-18 Homologues of bacterial TnpB_IS605 are widespread in diverse eukaryotic transposable elements Bao, Weidong Jurka, Jerzy Mob DNA Research BACKGROUND: Bacterial insertion sequences (IS) of IS200/IS605 and IS607 family often encode a transposase (TnpA) and a protein of unknown function, TnpB. RESULTS: Here we report two groups of TnpB-like proteins (Fanzor1 and Fanzor2) that are widespread in diverse eukaryotic transposable elements (TEs), and in large double-stranded DNA (dsDNA) viruses infecting eukaryotes. Fanzor and TnpB proteins share the same conserved amino acid motif in their C-terminal half regions: D-X(125, 275)-[TS]-[TS]-X-X-[C4 zinc finger]-X(5,50)-RD, but are highly variable in their N-terminal regions. Fanzor1 proteins are frequently captured by DNA transposons from different superfamilies including Helitron, Mariner, IS4-like, Sola and MuDr. In contrast, Fanzor2 proteins appear only in some IS607-type elements. We also analyze a new Helitron2 group from the Helitron superfamily, which contains elements with hairpin structures on both ends. Non-autonomous Helitron2 elements (CRe-1, 2, 3) in the genome of green alga Chlamydomonas reinhardtii are flanked by target site duplications (TSDs) of variable length (approximately 7 to 19 bp). CONCLUSIONS: The phylogeny and distribution of the TnpB/Fanzor proteins indicate that they may be disseminated among eukaryotic species by viruses. We hypothesize that TnpB/Fanzor proteins may act as methyltransferases. BioMed Central 2013-04-01 /pmc/articles/PMC3627910/ /pubmed/23548000 http://dx.doi.org/10.1186/1759-8753-4-12 Text en Copyright © 2013 Bao and Jurka; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Bao, Weidong Jurka, Jerzy Homologues of bacterial TnpB_IS605 are widespread in diverse eukaryotic transposable elements |
title | Homologues of bacterial TnpB_IS605 are widespread in diverse eukaryotic transposable elements |
title_full | Homologues of bacterial TnpB_IS605 are widespread in diverse eukaryotic transposable elements |
title_fullStr | Homologues of bacterial TnpB_IS605 are widespread in diverse eukaryotic transposable elements |
title_full_unstemmed | Homologues of bacterial TnpB_IS605 are widespread in diverse eukaryotic transposable elements |
title_short | Homologues of bacterial TnpB_IS605 are widespread in diverse eukaryotic transposable elements |
title_sort | homologues of bacterial tnpb_is605 are widespread in diverse eukaryotic transposable elements |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3627910/ https://www.ncbi.nlm.nih.gov/pubmed/23548000 http://dx.doi.org/10.1186/1759-8753-4-12 |
work_keys_str_mv | AT baoweidong homologuesofbacterialtnpbis605arewidespreadindiverseeukaryotictransposableelements AT jurkajerzy homologuesofbacterialtnpbis605arewidespreadindiverseeukaryotictransposableelements |