A1 Refereed original research article in a scientific journal
The core domain of retrotransposon integrase in Hordeum: Predicted structure and evolution
Authors: Suoniemi A, Tanskanen J, Pentikainen O, Johnson MS, Schulman AH
Publisher: OXFORD UNIV PRESS
Publication year: 1998
Journal: Molecular Biology and Evolution
Journal name in source: MOLECULAR BIOLOGY AND EVOLUTION
Journal acronym: MOL BIOL EVOL
Volume: 15
Issue: 9
First page : 1135
Last page: 1144
Number of pages: 10
ISSN: 0737-4038
DOI: https://doi.org/10.1093/oxfordjournals.molbev.a026021(external)
Abstract
Propagation of long terminal repeat (LTR)-bearing retrotransposons and retroviruses requires integrase (LN, EC 2.7.7.-), encoded by the retroelements themselves, which mediates the insertion of cDNA copies back into the genome. An active retrotransposon family, BARE-1, comprises similar to 7% of the barley (Hordeum vulgare subsp. vulgare) genome. We have generated models for the secondary and tertiary structure of BARE-I IN and demonstrate their similarity to structures for human immunodeficiency virus 1 and avian sarcoma virus INs. The IN core domains were compared for 80 clones from 28 Hordeum accessions representative of the diversity of the genus. Based on the structural model, variations in the predicted, aligned translations from these clones would have minimal structural and functional effects on the encoded enzymes. This indicates that Hordeum retrotransposon IN has been under purifying selection to maintain a structure typical of retroviral INs. These represent the first such analyses for plant INs.
Propagation of long terminal repeat (LTR)-bearing retrotransposons and retroviruses requires integrase (LN, EC 2.7.7.-), encoded by the retroelements themselves, which mediates the insertion of cDNA copies back into the genome. An active retrotransposon family, BARE-1, comprises similar to 7% of the barley (Hordeum vulgare subsp. vulgare) genome. We have generated models for the secondary and tertiary structure of BARE-I IN and demonstrate their similarity to structures for human immunodeficiency virus 1 and avian sarcoma virus INs. The IN core domains were compared for 80 clones from 28 Hordeum accessions representative of the diversity of the genus. Based on the structural model, variations in the predicted, aligned translations from these clones would have minimal structural and functional effects on the encoded enzymes. This indicates that Hordeum retrotransposon IN has been under purifying selection to maintain a structure typical of retroviral INs. These represent the first such analyses for plant INs.
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