High impact information on NDPK1

• The structure of Arabidopsis NDPK1 and NDPK2 showed that the isoforms share common electrostatic surfaces at the nucleotide-binding site, but the variable C-terminal regions have distinct electrostatic charge distributions [1].
• To resolve the controversy of whether serine/threonine phosphorylation of NDPK occurs as has been suggested by other NDPK studies, NDPK2 putative phosphorylation site mutants were generated and examined [2].
• Nucleoside diphosphate kinase III is localized to the inter-membrane space in plant mitochondria [3].
• Analysis of the deduced amino acid sequence confirmed its identity with the sequences obtained from the purified mature pea mitochondrial NDPK [4].
• Recently we isolated three NDPK cDNAs from Chinese cabbage cDNA library [5].

Biological context of NDPK1

• Nucleoside diphosphate kinase is a possible component of the ethylene signal transduction pathway [6].

Associations of NDPK1 with chemical compounds

• Phosphorylation of this protein was upregulated by ethylene but nucleoside diphosphate kinase activity was unaffected [7].
• Using the receptor-directed antagonist of ethylene action 2,5-norbornadiene and the ethylene-insensitive mutants of A. thaliana etr1-1 and eti5, ethylene specificity and receptor dependence of NDPK phosphorylation have been demonstrated [6].

Analytical, diagnostic and therapeutic context of NDPK1

• Amplification of a 317 nt product was performed by PCR, using oligonucleotide primers based on partial amino acid sequences of the pea mitochondria NDPK and other NDPK isoforms [4].

References