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Crystal structure of Arabidopsis thaliana calmodulin7 and insight into its mode of DNA binding
Author(s) -
Kumar Sanjeev,
Mazumder Mohit,
Gupta Nisha,
Chattopadhyay Sudip,
Gourinath Samudrala
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12349
Subject(s) - arabidopsis thaliana , dna , arabidopsis , calmodulin , transcription factor , gene isoform , chemistry , guanine , microbiology and biotechnology , dna binding protein , biochemistry , biology , nucleotide , gene , mutant , enzyme
Calmodulin (CaM) is a Ca 2+ sensor that participates in several cellular signaling cascades by interacting with various targets, including DNA . It has been shown that Arabidopsis thaliana CaM7 (AtCaM7) interacts with Z‐box DNA and functions as a transcription factor [Kushwaha R et al . (2008) Plant Cell 20, 1747–1759; Abbas N et al . (2014) Plant Cell 26, 1036–1052]. The crystal structure of AtCaM7, and a model of the At CAM 7‐Z‐box complex suggest that Arg‐127 determines the DNA ‐binding ability by forming crucial interactions with the guanine base. We validated the model using biolayer interferometry, which confirmed that AtCaM7 interacts with Z‐box DNA with high affinity. In contrast, the AtCaM2/3/5 isoform does not show any binding, although it differs from AtCaM7 by only a single residue.