A Caltech Library Service

Genomic and cDNA clones for maize phosphoenolpyruvate carboxylase and pyruvate,orthophosphate dikinase: Expression of different gene-family members in leaves and roots

Hudspeth, Richard L. and Glackin, Carlotta A. and Bonner, James and Grula, John W. (1986) Genomic and cDNA clones for maize phosphoenolpyruvate carboxylase and pyruvate,orthophosphate dikinase: Expression of different gene-family members in leaves and roots. Proceedings of the National Academy of Sciences of the United States of America, 83 (9). pp. 2884-2888. ISSN 0027-8424. PMCID PMC323411. doi:10.1073/pnas.83.9.2884.

PDF - Published Version
See Usage Policy.


Use this Persistent URL to link to this item:


We have isolated cDNA clones for the maize leaf enzymes phosphoenolpyruvate (P-ePrv) carboxylase [orthophosphate:oxaloacetate carboxy-lyase (phosphorylating) EC] and pyruvate,orthophosphate (Prv,Pi) dikinase (ATP:pyruvate,orthophosphate phosphotransferase, EC by exploiting the light-inducibility and large size of the mRNAs (3.5 kilobases) that encode the two enzymes. The clones were identified by hybrid-selection and immunoprecipitation assays. From a maize genomic library, two different types of genomic clones were screened with both the P-ePrv carboxylase and the Prv,Pi dikinase cDNA clones. Information from these genomic clones and genome blots indicates that the P-ePrv carboxylase gene family has at least three members and the Prv,Pi dikinase family at least two. Transcripts for both enzymes were detected in green leaves, etiolated leaves, and roots. The results show that the P-ePrv carboxylase mRNAs in green leaves and roots are encoded by different genes. Whereas the P-ePrv carboxylase mRNAs in all three tissues appear to be the same size, the Prv,Pi dikinase mRNA in green leaves is about 0.5 kilobases longer than the Prv,Pi dikinase mRNAs in etiolated leaves and roots. It is possible that all these Prv,Pi dikinase transcripts are encoded by one gene, and the size differences may correspond to the presence or absence of a sequence encoding a chloroplast transit peptide.

Item Type:Article
Related URLs:
URLURL TypeDescription CentralArticle
Additional Information:© 1986 by the National Academy of Sciences. Contributed by James Bonner, December 18, 1985. We thank Dr. Tatsuo Sugiyama for antiserum against maize leaf Prv,Pi dikinase and Dr. Hans Lehrach for EMBL phage vectors and host strains. Drs. Richard Yenofsky, Constantin Flytzanis, and David Anderson provided valuable information on various procedures. We thank Drs. Robert Goldberg, Richard Yenofsky, and David Anderson for very helpful criticism of the work while in progress and of the manuscript. Mary Strother and Elizabeth Hanson assisted in the manuscript preparation. This work was supported by Eli Lilly and Company (Indianapolis, IN) and the J.G. Boswell Company (Los Angeles). The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.
Funding AgencyGrant Number
James G. Boswell FoundationUNSPECIFIED
Subject Keywords:photosynthesis; enzymes; light-regulation; tissue specificity
Issue or Number:9
PubMed Central ID:PMC323411
Record Number:CaltechAUTHORS:HUDpnas86
Persistent URL:
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:8836
Deposited By: Tony Diaz
Deposited On:20 Sep 2007
Last Modified:08 Nov 2021 20:53

Repository Staff Only: item control page