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United States Department of Agriculture

Agricultural Research Service

Title: Nucleotide and Deduced Amino Acid Sequences of the Pyruvate Dehydrogenase Kinase from Arabidopsis Thaliana (Accession No. Af039406)

Authors
item Thelen, Jay - U OF MO, COLUMBIA, MO
item Miernyk, Jan
item Randall, Douglas - U OF MO, COLUMBIA, MO

Submitted to: Plant Physiology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: July 9, 1999
Publication Date: N/A

Interpretive Summary: Respiration can be thought of as the use of energy by living cells to do work. Important components of this work include growth and reproduction. Respiration must be carefully controlled or energy will be wasted. Wasted energy would decrease crop yields and reduce agricultural productivity. The control of respiration in plant cells is not yet fully understood. The genetic material for an important control step in respiration was isolated from the model plant, thalecress, and studied. Comparisons were made with similar genetic material from animals, in order to identify which parts might be important in control of respiration. A method was developed to prepare large amounts of the plant products that had full biological activity. Being able to produce large amounts of material will allow detailed analysis of the structures. This information will be important to researchers in their attempts to increase agricultural productivity by altering the control of plant cell respiration, and to other plant scientists who will try to design more efficient crop plants through either classical breeding or biotechnology.

Technical Abstract: Using the sequence of the previously characterized maize mitochondrial pyruvate dehydrogenase kinase (Thelen et al., 1998) as the search criterion, an Arabidopsis thaliana expressed sequence tag clone encoding pyruvate dehydrogenase kinase was identified. This cDNA clone was completely sequenced in both directions. The primary amino acid sequence was 77% identical to maize pyruvate dehydrogenase kinase 1, and 25 to 33 % identical with mammalian pyruvate dehydrogenase kinase sequences. The protein structure is more closely related to prokaryotic protein histidine-kinases than it is to protein serine/threonine kinases. A histidine residue thought to be the site of autophosphorylation was identified. The results of Southern analyses are consistent with the occurrence of a single structural gene.

Last Modified: 10/20/2014
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