Please use this identifier to cite or link to this item:
http://223.31.159.10:8080/jspui/handle/123456789/884
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Jamsheer, K Muhammed | - |
dc.contributor.author | Shukla, Brihaspati N. | - |
dc.contributor.author | Jindal, Sunita | - |
dc.contributor.author | Gopan, Nandu | - |
dc.contributor.author | Mannully, Chanchal Thomas | - |
dc.contributor.author | Laxmi, Ashverya | - |
dc.date.accessioned | 2018-09-09T09:19:03Z | - |
dc.date.available | 2018-09-09T09:19:03Z | - |
dc.date.issued | 2018 | - |
dc.identifier.citation | Journal of Biological Chemistry, 293(34): 13134-13150 | en_US |
dc.identifier.issn | 1083-351X | - |
dc.identifier.uri | http://223.31.159.10:8080/jspui/handle/123456789/884 | - |
dc.description | Accepted date: June 26, 2018 | en_US |
dc.description.abstract | The SNF1-related protein kinase 1 (SnRK1) is a heterotrimeric eukaryotic kinase that interacts with diverse proteins and regulates their activity in response to starvation and stress signals. Recently, the FCS-like zinc finger (FLZ) proteins were identified as a potential scaffold for SnRK1 in plants. However, the evolutionary and mechanistic aspect of this complex formation is currently unknown. Here, in silico analyses predicted that FLZ proteins possess conserved intrinsically disordered regions (IDRs) with a propensity for protein binding in the N and C termini across the plant lineage. We observed that the Arabidopsis FLZ proteins promiscuously interact with SnRK1 subunits, which formed different isoenzyme complexes. The FLZ domain was essential for mediating the interaction with SnRK1α subunits, whereas the IDRs in the N termini facilitated interactions with the β and βγ subunits of SnRK1. Furthermore, the IDRs in the N termini were important for mediating dimerization of different FLZ proteins. Of note, the interaction of FLZ with SnRK1 was confined to cytoplasmic foci, which colocalized with the endoplasmic reticulum. An evolutionary analysis revealed that in general, the IDR-rich regions are under more relaxed selection than the FLZ domain. In summary, the findings in our study reveal the structural details, origin, and evolution of a land plant–specific scaffold of SnRK1 formed by the coordinated actions of IDRs and structured regions in the FLZ proteins. We propose that the FLZ protein complex might be involved in providing flexibility, thus enhancing the binding repertoire of the SnRK1 hub in land plants. | en_US |
dc.description.sponsorship | Authors acknowledge NIPGR Confocal Facility for their assistance in microscopy. This work was financially supported by a Project Grant from the Department of Biotechnology, Government of India (Grant no. BT/PR8001/BRB/10/1211/2013) and a Core Grant from the National Institute of Plant Genome Research. MJK acknowledges University Grants Commission, Government of India for the research fellowship. MJK and CTM acknowledge National Institute of Plant Genome Research for the research fellowship. SJ acknowledges the research fellowship from the Project Grant from the Department of Biotechnology, Government of India (Grant no. BT/PR12855/BPA/118/87/2015). | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | The American Society for Biochemistry and Molecular Biology | en_US |
dc.subject | Computational biology | en_US |
dc.subject | protein complex | en_US |
dc.subject | scaffold protein | en_US |
dc.subject | intrinsically disordered regions | en_US |
dc.subject | zinc finger | en_US |
dc.subject | SnRK1 | en_US |
dc.subject | protein evolution | en_US |
dc.subject | land plants | en_US |
dc.title | The FCS-like zinc finger scaffold of the kinase SnRK1 is formed by the coordinated actions of the FLZ domain and intrinsically disordered regions | en_US |
dc.type | Article | en_US |
dc.identifier.officialurl | http://www.jbc.org/content/293/34/13134 | en_US |
dc.identifier.doi | doi: 10.1074/jbc.RA118.002073 | en_US |
Appears in Collections: | Institutional Publications |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Laxmi A_2018_2.pdf Restricted Access | 7.02 MB | Adobe PDF | View/Open Request a copy |
Items in IR@NIPGR are protected by copyright, with all rights reserved, unless otherwise indicated.