1H, 13C, 15N backbone and side chain NMR resonance assignments for the N-terminal RNA recognition motif of the HvGR-RBP1 protein involved in the regulation of barley (Hordeum vulgare L.) senescence

Biomolecular NMR Assignments

Volumn 8, Issue 1, 2014, Pages 149-153

  Mason, Katelyn E ^a   Tripet, Brian P ^a   Parrott, David ^a   Fischer, Andreas M ^a   Copié, Valérie ^a  

^a MONTANA STATE UNIVERSITY   (United States)

Author keywords

Barley; Hordeum vulgare L. barley strain; HvGR RBP1 barley protein; NMR; Plant senescence; Protein structure function; RNA recognition motif; RNA binding protein

Indexed keywords

CARBON; HYDROGEN; NITROGEN; VEGETABLE PROTEIN;

ARTICLE; CHEMISTRY; GROWTH, DEVELOPMENT AND AGING; HORDEUM; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE;

AMINO ACID MOTIFS; CARBON ISOTOPES; HORDEUM; HYDROGEN; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PLANT PROTEINS; PROTEIN STRUCTURE, SECONDARY;

EID: 84897112512     PISSN: 18742718     EISSN: 1874270X     Source Type: Journal    
DOI: 10.1007/s12104-013-9472-8     Document Type: Article

References (11)

1. Clery A, Blatter M, Allain F (2008) RNA recognition motifs: Boring? Not quite. Curr Opin Struct Biol 18:290-298
2. Corbin-Lickfett KA, Souki SK, Cocco MJ, Sandri-Goldin RM (2010) Three arginine residues within the RGG box are crucial for ICP27 binding to herpes simplex virus 1 GC-rich sequences and for efficient viral RNA export. J Virol 84:6367-6376
3. Delaglio F, Grzesiek S, Vuister G, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277-293
4. Gregersen PL, Holm PB, Krupinska K (2008) Leaf senescence and nutrient remobilisation in barley and wheat. Plant Biol (Stuttg) 10(Suppl 1):37-49
5. Jukanti A, Heidlebaugh N, Parrott D, Fischer I, McInnerney K, Fischer A (2008) Comparative transcriptome profiling of near-isogenic barley (Hordeum vulgare) lines differing in the allelic state of a major grain protein content locus identifies genes with possible roles in leaf senescence and nitrogen reallocation. New Phytol 177:333-349
6. Kuwasako K, Takahashi M, Tochio N, Abe C, Tsuda K, Inoue M, Terada T, Shirouzu M, Kobayashi N, Kigawa T, Taguchi S, Tanaka A, Hayashizaki Y, Guntert P, Muto Y, Yokoyama S (2008) Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode. Biochemistry 47:6437-6450
7. Maris C, Dominguez C, Allain F (2005) The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression. FEBS J 272:2118-2131
8. Schlenker C, Goel A, Tripet B, Menon S, Willi T, Dlakic M, Young M, Lawrence M, Copie V (2012) Structural studies of E73 from a hyperthermophilic archaeal virus identify the, RH3, alpha domain, an elaborated ribbon, helix, helix motif involved in DNA recognition. Biochemistry 51:2899-2910
9. See D, Kanazin V, Kephart K, Blake T (2002) Mapping genes controlling variation in barley grain protein concentration. Crop Sci 42:680
10. Tripet B, Goel A, Copié V (2011) Internal dynamics of the tryptophan repressor (TrpR) and two functionally distinct TrpR variants, L75F-TrpR and A77 V-TrpR, in their l-Trp-bound forms. Biochemistry 23:5140-5153
11. Wishart D, Nip A (1998) Protein chemical shift analysis: A practical guide. Biochem Cell Biol 76:153-163