Phosphorylated nitrate reductase and 14-3-3 proteins: Site of interaction, effects of ions, and evidence for an AMP-binding site on 14-3-3 proteins

Plant Physiology

Volumn 118, Issue 3, 1998, Pages 1041-1048

  Athwal, Gurdeep S ^a   Huber, Joan L ^a   Huber, Steven C ^b  

^a AGRICULTURAL RESEARCH SERVICE   (United States)

^b NORTH CAROLINA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE PHOSPHATE; NITRATE REDUCTASE; PEPTIDE; PROTEIN; PROTEIN 14 3 3; SERINE; TYROSINE 3 MONOOXYGENASE;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CHEMISTRY; ENZYMOLOGY; METABOLISM; MOLECULAR GENETICS; NON-PROGRAMMATIC; PHOSPHORYLATION; PROTEIN BINDING; SEQUENCE HOMOLOGY; SPINACH;

NON-PROGRAMMATIC;

14-3-3 PROTEINS; ADENOSINE MONOPHOSPHATE; AMINO ACID SEQUENCE; BINDING SITES; MOLECULAR SEQUENCE DATA; NITRATE REDUCTASE; NITRATE REDUCTASES; PEPTIDES; PHOSPHORYLATION; PROTEIN BINDING; PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SERINE; SPINACIA OLERACEA; TYROSINE 3-MONOOXYGENASE;

EID: 0032197397     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.118.3.1041     Document Type: Article

References (8)

1. Aitken A (1996) 14-3-3 and its possible role in co-ordinating multiple signalling pathways. Trends Cell Biol 6: 341-347
2. Bachmann M, Huber JL, Athwal GS, Wu K, Ferl RJ, Huber SC (1996a) 14-3-3 proteins associated with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform-specific manner and reduced dephosphorylation of Ser-543 by endogenous protein phosphatases. FEBS Lett 398: 26-30
3. Bachmann M, Huber JL, Liao P-C, Gage DA, Huber SC (1996b) The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14-3-3 protein. FEBS Lett 387: 127-131
4. Bachmann M, McMicheal RW Jr, Huber JL, Kaiser WM, Huber SC (1995) Partial purification and characterization of a calcium-dependent protein kinase and an inhibitor protein required for inactivation of spinach leaf nitrate reductase. Plant Physiol 108: 1083-1091
5. Lu G, Sehnke PC, Ferl RJ (1994) Phosphorylation and calcium binding properties of an Arabidopsis GF14 brain protein homolog. Plant Cell 6: 501-510
6. McMichael RW, Bachmann M, Huber SC (1995) Spinach leaf sucrose-phosphate synthase and nitrate reductase are phosphorylated/inactivated by multiple protein kinases in vitro. Plant Physiol 108: 1077-1082
7. Wu K, Lu G, Sehnke P, Ferl RJ (1997) The heterologous interaction among plant 14-3-3 proteins and identification of regions that are important for dimerization. Arch Biochem Biophys 339: 2-8
8. Yaffe MB, Rittinger K, Volinia S, Caron PR, Aitken A, Leffers H, Gamblin SJ, Smerdon SJ, Cantley LC (1997) The structural basis for 14-3-3: phosphopeptide binding specificity. Cell 91: 961-971