|Citation||Kapitonov, V.V., Jurka, J. (2003). The esterase and PHD domains in CR1-like non-LTR retrotransposons. Mol. Biol. Evol. 20(1): 38--46. (Export to RIS)|
|Publication Type||Research paper|
|PubMed Abstract||Most active non-LTR (long terminal repeat) retrotransposons carry two open reading frames (ORFs) encoding ORF1p and ORF2p proteins. The ORF2p proteins are relatively well studied and are known to contain endonuclease/reverse transcriptase domains. At the same time, the biological function of ORF1p proteins remains poorly understood, except in that they nonspecifically bind single-stranded mRNA/DNA molecules. CR1-like elements form the most widely distributed clade/superfamily of non-LTR retrotransposons. We found that ORF1p proteins encoded by diverse CR1-like elements contain conserved esterase domain (ES) or plant homeodomain (PHD). This indicates that CR1-like ORF1p proteins are either lipolytic enzymes or are involved in protein-protein interactions related to chromatin remodeling. Sequence conservation of ES suggests that interaction with cellular membranes is an important phase in life circles of CR1-like elements. Presumably such interaction helps in penetrating host cells. As a consequence, the presence of multiple young CR1 families characterized by approximately 10% intrafamily and 40% interfamily identities may be explained by a relatively frequent horizontal transfer of these CR1-like elements. Unexpectedly, ES links together non-LTR retrotransposons and single-stranded RNA viruses like influenza C and coronaviruses, which are known to depend on their own ES.|
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|Language of Publication||English|
|Additional Languages of Abstract|
|Also Published As|
|Abbreviation||Mol. Biol. Evol.|
|Title||Molecular Biology and Evolution|
|Data from Reference|
|Natural transposons (5)|