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- Publisher
- Springer Journals
- Copyright
- Copyright © 2011 by Springer Science+Business Media B.V.
- Subject
- Physics; Polymer Sciences; Biochemistry, general; Biophysics and Biological Physics
- ISSN
- 1874-2718
- eISSN
- 1874-270X
- DOI
- 10.1007/s12104-011-9313-6
- pmid
- 21553305
- Publisher site
- See Article on Publisher Site
Abstract
VERNALIZATION1 (VRN1) is a multidomain DNA binding protein from Arabidopsis thaliana that is required for the acceleration of flowering time in response to prolonged cold treatment; a physiological process called vernalization. VRN1 is a 39 kDa protein comprised of two B3 domains flanking a putative nuclear localization sequence and two PEST domains. Here we report the 1H, 13C and 15N resonance assignments of the 134 residue C-terminal region of VRN1, comprising a B3 DNA binding domain of the REM family and an upstream region that is highly conserved among VRN1 homologs from other dicotyledonous plant species.
Journal
Biomolecular NMR Assignments – Springer Journals
Published: May 8, 2011