Record Details

The FCS-like zinc finger scaffold of the kinase SnRK1 is formed by the coordinated actions of the FLZ domain and intrinsically disordered regions

NIPGR Digital Knowledge Repository (NDKR)

View Archive Info
 
 
Field Value
 
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
 
Creator Jamsheer, K Muhammed
Shukla, Brihaspati N.
Jindal, Sunita
Gopan, Nandu
Mannully, Chanchal Thomas
Laxmi, Ashverya
 
Subject Computational biology
protein complex
scaffold protein
intrinsically disordered regions
zinc finger
SnRK1
protein evolution
land plants
 
Description Accepted date: June 26, 2018
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.
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).
 
Date 2018-09-09T09:19:03Z
2018-09-09T09:19:03Z
2018
 
Type Article
 
Identifier Journal of Biological Chemistry, 293(34): 13134-13150
1083-351X
http://223.31.159.10:8080/jspui/handle/123456789/884
http://www.jbc.org/content/293/34/13134
doi: 10.1074/jbc.RA118.002073
 
Language en_US
 
Format application/pdf
 
Publisher The American Society for Biochemistry and Molecular Biology