Abstract
In leucine-rich repeat (LRR) receptor-like kinase XI subfamily, Arabidopsis HAESA (AtHAE) and two closely related HAESA-LIKE (AtHSL1 and AtHSL2) constitute a small branch. Several reports have described the function and the involved signaling pathway that AtHAE and AtHSLs are involved in. However, the family members and functions of HAE and HSL in rice have not been reported. Here, we performed a genome-wide analysis of the HAE/HSL kinase family in rice. A total of 17 OsHSLs were identified in the genome. Of these, only Os11g11890 was annotated as HSL2; all the other members were annotated as HSL1. Phylogenetic analysis revealed that OsHSLs diverged into three groups, with three Arabidopsis members constituting a subgroup of group I. Domain analysis revealed that all the homologues had 9-19 LRR repeats and a typical kinase domain at the C-terminus, except that four members lost or evolved their kinase domains. Expression analysis revealed that OsHSLs were co-expressed with genes involved in biotic and abiotic stresses. Microarray data revealed that most OsHSLs were highly expressed in the vegetative tissues and only two members were highly expressed in the reproductive tissues. Most OsHSLs changed their expression profiles when subjected to drought, and salt stress treatments. Our results provide an overview of OsHSL gene family in rice, and suggest that OsHSLs possibly function under biotic and abiotic stresses, thus would help for elucidating the function of OsHSLs gene family in vivo.
Highlights
IntroductionThese signal transductions are usually accomplished by reversible phosphorylation of protein kinases (PKs)
Only Os11g11890 had been annotated as HSL2, while all the other sequences had been annotated as HSL1 (Table 1)
Only Os11g11890 had been annotated as HSL2, all the other sequences had been annotated as HSL1
Summary
These signal transductions are usually accomplished by reversible phosphorylation of protein kinases (PKs). As the substrates and functions of most PKs in plants have not been identified, plant PKs were temporarily named receptor-like kinases (RLKs) [1]. RLKs can be divided into several families according to their extracellular domains. The LRR domain is generally 20 - 30 amino acids long, and forms α/β helix. These structural characteristics allow LRR-RLKs to participate in protein-protein interactions, whereby modulating cellular functions such as signal transductions, stress response, and immunity [1]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
