Conserved and unique features of the homeologous maize Aux/IAA proteins ROOTLESS WITH UNDETECTABLE MERISTEM 1 and RUM1-like 1
| Autor: | Kenneth W. Berendzen, Huanhuan Tai, Caroline Marcon, Inga von Behrens, Yvonne Ludwig, Yanxiang Zhang, Frank Hochholdinger, Stefan Hey |
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| Rok vydání: | 2015 |
| Předmět: |
0106 biological sciences
0301 basic medicine RUL1 Physiology Sequence alignment Aux/IAA Plant Science Biology maize Zea mays 01 natural sciences 03 medical and health sciences Bimolecular fluorescence complementation Gene Expression Regulation Plant Auxin protein interaction Amino Acid Sequence Gene Peptide sequence Plant Proteins chemistry.chemical_classification RAP1 RUM1 food and beverages Meristem root Amino acid 030104 developmental biology chemistry Biochemistry Degron Sequence Alignment Research Paper 010606 plant biology & botany |
| Zdroj: | Journal of Experimental Botany |
| ISSN: | 1460-2431 0022-0957 |
| DOI: | 10.1093/jxb/erv519 |
| Popis: | Highlight The maize Aux/IAA protein RUM1 and its homeolog RUL1 display conserved biochemical properties. The specific interaction of RAP1 with RUM1 but not RUL1 suggests differences in their molecular interactions. The maize (Zea mays L.) Aux/IAA protein RUM1 (ROOTLESS WITH UNDETECTABLE MERISTEM 1) is a key regulator of lateral and seminal root formation. An ancient maize genome duplication resulted in the emergence of its homeolog rum1-like1 (rul1), which displays 92% amino acid sequence identity with RUM1. Both, RUL1 and RUM1 exhibit the canonical four domain structure of Aux/IAA proteins. Moreover, both are localized to the nucleus, are instable and have similar short half-lives of ~23min. Moreover, RUL1 and RUM1 can be stabilized by specific mutations in the five amino acid degron sequence of domain II. In addition, proteins encoded by both genes interact in vivo with auxin response factors (ARFs) such as ZmARF25 and ZmARF34 in protoplasts. Although it was demonstrated that RUL1 and RUM1 can homo and heterodimerize in vivo, rul1 expression is independent of rum1. Moreover, on average rul1 expression is ~84-fold higher than rum1 in the 12 tested tissues and developmental stages, although the relative expression levels in different root tissues are very similar. While RUM1 and RUL1 display conserved biochemical properties, yeast-two-hybrid in combination with BiFC experiments identified a RUM1-associated protein 1 (RAP1) that specifically interacts with RUM1 but not with RUL1. This suggests that RUM1 and RUL1 are at least in part interwoven into different molecular networks. |
| Databáze: | OpenAIRE |
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