Nucleoside diphosphate kinase (NDPK) operates in the homeostasis of cellular nucleoside triphosphate (NTP) pools and the cytosolic NDPK1 is the main NDPK isoform in plants, accounting for more than 70 % of total NDPK activity in plant. A full length cDNA (697 bp), designated as CsNDPK1 was cloned from Camellia sinensis (L.) O. Kuntze leaves. Sequence analysis of CsNDPK1 shows several motifs, binding and catalytic sites which are highly conserved among other NDPKs. Southern blot analysis revealed that tea genome has two copies of CsNDPK1. Transcription pattern analysis indicated that CsNDPK1 is expressed in all tissues examined, but expressed more in buds than in other organs. © 2012 Springer Science+Business Media B.V.

Abul Kalam Azad Mandal

Department of Biotechnology

School of Bio Sciences and Technology

Vellore Campus

Prabu G.R

Thirugnanasambantham K

Saravanan A.

Vellore Institute of Technology (VIT) is a private university located in&nbsp;Tamil Nadu, India. Founded in 1984, as Vellore Engineering College, the institution offers 20 undergraduate, 34 postgraduate, four integrated and four research programs. It has campuses in Vellore, Amravati, Bhopal and Chennai.

VIT is one of the top ranked private universities in India according to NIRF, THE and QS Rankings.&nbsp;Govt. of India has recognized&nbsp;VIT, Vellore as an&nbsp;Institution of Eminence. This has allowed VIT to take independent quality initiatives and move up in world ranking.

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VIT University

Biologia plantarum

Nucleoside diphosphate kinase (NDPK, EC 2.7.4.6) is a housekeeping gene, which functions in the general homeostasis of cellular nucleoside triphosphate (NTP) pools. Among the various NDPK isoforms, cytosolic NDPK1 has been shown to be the main NDPK isoform in plants, accounting for more than 70 % of total NDPK activity in plants. For the first time, a full-length cDNA (697 bp), designated as CsNDPK1 was cloned from tea leaves and consisted of a 448-bp open reading frame (ORF) encoding a 147-amino-acid polypeptide with calculated molecular mass of 16.1 kDa and a pI of 6.3. Homology modeling of CsNDPK1 shows that the presented tea NDPK1 also contains several motifs, binding and catalytic sites which are highly conserved among other NDPKs. Docking studies of CsNDPK1 with its substrates (NTPs) are discussed in detail. In summary, we describe a reliable model of CsNDPK1 that can be used in structure-based protein-protein interaction studies for identifying its potential role in intracellular communication and its physiological significance in tea. © 2012 Springer Science+Business Media New York.

Applied Biochemistry and Biotechnology

Structural and Docking Studies of a Nucleoside Diphosphate Kinase 1 (CsNDPK1) from Tea [Camellia sinensis (L.) O. Kuntze]

Plant Science

The activities of nucleoside diphosphate kinase and adenylate kinase are influenced by their interaction

Frontiers of Agriculture in China

Research progress on isolation and cloning of functional genes in tea plants

Molecular Biology and Evolution

MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) Software Version 4.0

Planta

Characterization of a cytosolic nucleoside diphosphate kinase associated with cell division and growth in potato

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Nucleoside diphosphate kinase III is localized to the inter-membrane space in plant mitochondria

Molecular cloning and characterization of nucleoside diphosphate kinase 1 cDNA in tea

Journal	Biologia plantarum
Publisher	Institute of Experimental Botany
ISSN	0006-3134
Open Access	0