Extended Data Fig. 8: Sequences similar to NCR247.
From: A haem-sequestering plant peptide promotes iron uptake in symbiotic bacteria
a, UV-Vis spectrum of NCR peptides (NCR169, NCR035, NCR211, and NCR247) with heme indicating that only NCR247 shows a spectrum characteristic of heme binding proteins. b, Sequence alignment of NCR247 from the plants M. sativa and M. truncatula. c and d, Sequence alignment of NCR247 from M. truncatula and C-terminal region of DppD (protein involved in heme transport) of Hemophilus influenzae (c) and E. coli (d). In b, c, and d, alignments were performed using CLUSTAL Omega. NCR247 from M. sativa and C-terminal end of DppD were significantly similar sequences with a e-value less than 5 obtained in a BLAST search. e and f, Sequence similar to NCR247 from C-terminal end of DppD of E. coli, tagged to MBP purifies as a reddish colored protein (e) and shows EPR spectrum (mixture of high and low spin heme) similar to other haem binding proteins95 g and h, Chemically synthesized peptide with sequence similar to NCR247 from C-terminal end of DppD of H. influenzae shows reddish color upon binding heme (g) and exhibits a UV-Vis spectrum (366 nm, 427 nm, and 540 nm) characteristic of haem binding proteins(h). In a and e-h representative data from three independent experiments is shown.
