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Fig. 1 | BMC Plant Biology

Fig. 1

From: Conserved residues in the wheat (Triticum aestivum) NAM-A1 NAC domain are required for protein binding and when mutated lead to delayed peduncle and flag leaf senescence

Fig. 1

Identification of highly conserved residues of NAM-A1 in the cultivar Kronos TILLING population. Jensen-Shannon Divergence scores for a consensus alignment of NAC-domain-containing proteins from seven plant species (see methods) highlight the conserved nature of the 5 NAC subdomains, highlighted in grey (a, i-v). Residues present in fewer than 10% of sequences across the set of NAC transcription factors were excluded from the alignment. Previous work tested the role of specific residues in protein binding (subdomain i) and DNA binding (subdomains iii to v); residues required for the corresponding process are underlined in red, those not required are underlined in blue [24]. A histidine residue in subdomain iv plays a role in protein dimer stabilisation through interactions with part of the protein dimerization domain (subdomain i; both highlighted in green) [25]. The consensus NAC domain sequence obtained from this alignment is shown below the conservation scores (first line). The aligned NAC-domain of NAM-A1 is shown below the consensus sequence. Residues with missense mutations identified in the Kronos TILLING population are highlighted with a triangle (black). Note that the missense mutation in a non-conserved residue (C133Y) in K2551 is not present in the consensus alignment as it is not conserved across NAC proteins. Missense mutations, as well as non-conserved and synonymous controls (purple) and the splice acceptor variant K1107, are shown on a schematic of the NAM-A1 structure (b)

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