Plant Physiol. Tips for Better Browsing
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Plant Physiology 96:77-83 (1991)
© 1991 American Society of Plant Biologists

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hase, T.
Right arrow Articles by Sakakibara, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hase, T.
Right arrow Articles by Sakakibara, H.
Agricola
Right arrow Articles by Hase, T.
Right arrow Articles by Sakakibara, H.
Molecular Biology and Gene Regulation

Molecular Cloning and Differential Expression of the Maize Ferredoxin Gene Family 1

Toshiharu Hase, Yoko Kimata2, Keiko Yonekura3, Tomohiko Matsumura and Hitoshi Sakakibara

Department of Agricultural Chemistry, School of Agriculture, Nagoya University, Nagoya 464-01, Japan

In maize (Zea mays L.), four ferredoxin (Fd) isoproteins, Fd I to Fd IV, are differentially distributed in photosynthetic and nonphotosynthetic organs of young seedlings (Y Kimata, T Hase [1989] Plant Physiol 89: 1193-1197). To understand structural characteristics of the Fd isoproteins and molecular mechanism of the differential expression of their genes, we have cloned and characterized three different maize Fd cDNAs. DNA sequence analyses showed that two of the cDNAs encoded the entire precursor polypeptides of Fd I and Fd III, which were composed of 150 and 152 amino acid residues, respectively, and the other encoded a 135 amino acid precursor polypeptide of Fd not yet identified. High degrees of homologies were found in the deduced amino acid sequences of mature regions of these Fd isoproteins, but the transit peptide of Fd III differed considerably from those of other Fd isoproteins. Fd I and the unidentified Fd were encoded mainly with codons ending in C or G, but such strong codon bias was not seen in Fd III. Gene specific probes for each cDNA were used to probe Northern blots of RNA isolated from leaves, mesocotyls, and roots of maize seedlings. The gene transcripts for Fd I and the unidentified Fd were restricted to leaves and their levels increased markedly upon illumination of etiolated seedlings, whereas that for Fd III was detected in all organs and its accumulation was not light dependent. This organ specific accumulation of Fd mRNAs corresponds exactly to the distribution pattern of Fd isoproteins.


2 Present address: Department of Biochemistry, North Carolina State University, Raleigh, NC 27695-7622.

3 Present address: Plant Biotechnology Laboratory, Institute for Fundamental Research, Suntory Limited, Research Center, 1-1-1, Wakayamadai, Shimamoto-cho, Mishima-gun, Osaka 616, Japan.

1 This work was supported in part by Grant-in-Aid for Scientific Research (C) (Grant No. 02660086) from the Ministry of Education, Science, and Culture of Japan. This paper is dedicated to Professor Hiroshi Matsubara on the occasion of his sixtieth birthday.




This article has been cited by other articles:


Home page
J. Gen. Virol.Home page
Y.-Q. Cheng, Z.-M. Liu, J. Xu, T. Zhou, M. Wang, Y.-T. Chen, H.-F. Li, and Z.-F. Fan
HC-Pro protein of sugar cane mosaic virus interacts specifically with maize ferredoxin-5 in vitro and in planta
J. Gen. Virol., August 1, 2008; 89(8): 2046 - 2054.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Saitoh, T. Ikegami, M. Nakayama, K. Teshima, H. Akutsu, and T. Hase
NMR Study of the Electron Transfer Complex of Plant Ferredoxin and Sulfite Reductase: MAPPING THE INTERACTION SITES OF FERREDOXIN
J. Biol. Chem., April 14, 2006; 281(15): 10482 - 10488.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
G. Kurisu, D. Nishiyama, M. Kusunoki, S. Fujikawa, M. Katoh, G. T. Hanke, T. Hase, and K. Teshima
A Structural Basis of Equisetum arvense Ferredoxin Isoform II Producing an Alternative Electron Transfer with Ferredoxin-NADP+ Reductase
J. Biol. Chem., January 21, 2005; 280(3): 2275 - 2281.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
G. T. Hanke, Y. Kimata-Ariga, I. Taniguchi, and T. Hase
A Post Genomic Characterization of Arabidopsis Ferredoxins
Plant Physiology, January 1, 2004; 134(1): 255 - 264.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
S. Holtgrefe, K. P. Bader, P. Horton, R. Scheibe, A. von Schaewen, and J. E. Backhausen
Decreased Content of Leaf Ferredoxin Changes Electron Distribution and Limits Photosynthesis in Transgenic Potato Plants
Plant Physiology, December 1, 2003; 133(4): 1768 - 1778.
[Abstract] [Full Text]


Home page
Plant Physiol.Home page
T. Hirohashi, T. Hase, and M. Nakai
Maize Non-Photosynthetic Ferredoxin Precursor Is Mis-Sorted to the Intermembrane Space of Chloroplasts in the Presence of Light
Plant Physiology, April 1, 2001; 125(4): 2154 - 2163.
[Abstract] [Full Text]


Home page
Plant Physiol.Home page
D. J. Schultz, M. C. Suh, and J. B. Ohlrogge
Stearoyl-Acyl Carrier Protein and Unusual Acyl-Acyl Carrier Protein Desaturase Activities Are Differentially Influenced by Ferredoxin
Plant Physiology, October 1, 2000; 124(2): 681 - 692.
[Abstract] [Full Text]


Home page
Plant Physiol.Home page
Y. Onda, T. Matsumura, Y. Kimata-Ariga, H. Sakakibara, T. Sugiyama, and T. Hase
Differential Interaction of Maize Root Ferredoxin:NADP+ Oxidoreductase with Photosynthetic and Non-Photosynthetic Ferredoxin Isoproteins
Plant Physiology, July 1, 2000; 123(3): 1037 - 1046.
[Abstract] [Full Text]


Home page
Plant Physiol.Home page
K. Yonekura-Sakakibara, Y. Onda, T. Ashikari, Y. Tanaka, T. Kusumi, and T. Hase
Analysis of Reductant Supply Systems for Ferredoxin-Dependent Sulfite Reductase in Photosynthetic and Nonphotosynthetic Organs of Maize
Plant Physiology, March 1, 2000; 122(3): 887 - 894.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Akashi, T. Matsumura, T. Ideguchi, K.-i. Iwakiri, T. Kawakatsu, I. Taniguchi, and T. Hase
Comparison of the Electrostatic Binding Sites on the Surface of Ferredoxin for Two Ferredoxin-dependent Enzymes, Ferredoxin-NADP+ Reductase and Sulfite Reductase
J. Biol. Chem., October 8, 1999; 274(41): 29399 - 29405.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
T. Matsumura, Y. Kimata-Ariga, H. Sakakibara, T. Sugiyama, H. Murata, T. Takao, Y. Shimonishi, and T. Hase
Complementary DNA Cloning and Characterization of Ferredoxin Localized in Bundle-Sheath Cells of Maize Leaves
Plant Physiology, February 1, 1999; 119(2): 481 - 488.
[Abstract] [Full Text]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1991 by the American Society of Plant Biologists