ArticleJournal of experimental botany2016
Conserved and unique features of the homeologous maize Aux/IAA proteins ROOTLESS WITH UNDETECTABLE MERISTEM 1 and RUM1-like 1.
Article in Journal of experimental botany, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- NIN-LIKE PROTEIN3.2 inhibits repressor Aux/IAA14 expression and enhances root biomass in maize seedlings under low nitrogen.The Plant cell · 2024Article
- Article
- Paenibacillus lentimorbus alleviates nutrient deficiency-induced stress in Zea mays by modulating root system architecture, auxin signaling, and metabolic pathways.Plant cell reports · 2024Article
- Identification of a new QTL underlying seminal root number in a maize-teosinte population.Frontiers in plant science · 2023Article
- Maize Seedling Growth and Hormone Response Assays Using the Rolled Towel Method.Current protocols · 2022Article
- Deconstructing the root system of grasses through an exploration of development, anatomy and function.Plant, cell & environment · 2022Review
- Temporal and spatial auxin responsive networks in maize primary roots.Quantitative plant biology · 2022Article
- A Synthetic Approach Allows Rapid Characterization of the Maize Nuclear Auxin Response Circuit.Plant physiology · 2020Article
- Shared Genetic Control of Root System Architecture betweenPlant physiology · 2020Article
- The Quantitative Genetic Control of Root Architecture in Maize.Plant & cell physiology · 2018Article
- Dynamic Regulation of Auxin Response during Rice Development Revealed by Newly Established Hormone Biosensor Markers.Frontiers in plant science · 2017Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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