6nu4

Publication Abstract from PubMed

We report the recombinant preparation from Escherichia coli cells of samples of two closely related, small, secreted cysteine-rich plant peptides: Rapid ALkalinization Factor-1 (RALF1) and Rapid ALkalinization Factor-8 (RALF8). Purified samples of the native sequence of RALF8 exhibited well-resolved NMR spectra and also biological activity through interaction with a plant receptor kinase, cytoplasmic calcium mobilization, and in vivo root growth suppression. By contrast, RALF1 could only be isolated from inclusion bodies as a construct containing an N-terminal His-tag; its poorly resolved NMR spectrum was indicative of aggregation. We prepared samples of the RALF8 peptide labeled with (15) N and (13) C for NMR analysis and obtained near complete (1) H, (13) C, and (15) N NMR assignments, determined the disulfide pairing of its four cysteine residues, and examined its solution structure. RALF8 is mostly disordered except for the two loops spanned by each of its two disulfide bridges. This article is protected by copyright. All rights reserved.

Function and solution structure of the Arabidopsis thaliana RALF8 peptide.,Frederick RO, Haruta M, Tonelli M, Lee W, Cornilescu G, Cornilescu CC, Sussman MR, Markley JL Protein Sci. 2019 Apr 20. doi: 10.1002/pro.3628. PMID:31004454^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.