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A second form of adenine phosphoribosyltransferase in Arabidopsis thaliana with relative specificity towards cytokinins by Kirk Matthew Schnorr; Catherine Gaillard; Elisabeth Biget; Per Nygaard; Michel Laloue is a Agricultural and Biological Sciences article available to read on EtoBox.

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## Summary Adenine phosphoribosyltransferase (APRTase) is an important enzyme for its ability to convert adenine, a by‐product of many biochemical reactions, into AMP. By functional complementation of an __Escherichia coli__ mutant, cDNAs encoding two APRTases have been cloned from __Arabidopsis thaliana__. One of the cDNAs (__ATapt1__)has been previously identified while the second (__ATapt2__) is of a previously unknown type. Kinetic analysis of the two enzymes purified from __E. coli__ expressing the two cDNAs indicates that ATapt2 has a higher affinity for cytokinin than the ATapt1. RNase protection studies indicate that the __ATapt2__, is not expressed in leaves. Analysis of the gene structure indicates that __ATapt2__ has identical intron positions to __ATapt1__, but neither the intron sequence nor intron size are conserved between the two genes. The implications of a second, differentially expressed APRTase with affinity for both adenine and cytokinin are discussed.

Who reads A second form of adenine phosphoribosyltransferase in Arabidopsis thaliana with relative specificity towards cytokinins?

Author

Kirk Matthew Schnorr; Catherine Gaillard; Elisabeth Biget; Per Nygaard; Michel Laloue

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0960-7412)

Published

1996

Language

EN

Field

Agricultural and Biological Sciences (Life Sciences)