ATLs and BTLs, plant-specific and general eukaryotic structurally-related E3 ubiquitin ligases
Copyright © 2013 Elsevier Ireland Ltd. All rights reserved.
| Veröffentlicht in: | Plant science : an international journal of experimental plant biology. - 1985. - 215-216(2014) vom: 28. Feb., Seite 69-75 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2014
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| Zugriff auf das übergeordnete Werk: | Plant science : an international journal of experimental plant biology |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Review ATL E3 ubiquitin ligases Evolution of gene families RING fingers Rabring7/Bca2/BTLs uORFs Arabidopsis Proteins mehr... |
| Zusammenfassung: | Copyright © 2013 Elsevier Ireland Ltd. All rights reserved. Major components of the ubiquitin proteasome system are the enzymes that operate on the transfer of ubiquitin to selected target substrate, known as ubiquitin ligases. The RING finger is a domain that is present in key classes of ubiquitin ligases. This domain coordinates the interaction with a suitable E2 conjugase and the transfer of ubiquitin from the E2 to protein targets. Additional domains coupled to the same polypeptide are important for modulating the function of these ubiquitin ligases. Plants contain several types of E3 ubiquitin ligases that in many cases have expanded as multigene families. Some families are specific to the plant lineage, whereas others may have a common ancestor among plants and other eukaryotic lineages. Arabidopsis Tóxicos en Levadura (ATLs) and BCA2 zinc finger ATLs (BTLs) are two families of ubiquitin ligases that share some common structural features. These are intronless genes that encode a highly related RING finger domain, and yet during evolutionary history, their mode of gene expansion and function is rather different. In each of these two families, the co-occurrence of transmembrane helices or C2/C2 (BZF finger) domains with a selected variation on the RING finger has been subjected to strong selection pressure in order to preserve their unique domain architectures during evolution |
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| Beschreibung: | Date Completed 03.09.2014 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1873-2259 |
| DOI: | 10.1016/j.plantsci.2013.10.017 |