Osmotic stress induces expression of choline monooxygenase in sugar beet and amaranth

被引:99
作者
Russell, BL [1 ]
Rathinasabapathi, B [1 ]
Hanson, AD [1 ]
机构
[1] Univ Florida, Dept Hort Sci, Gainesville, FL 32611 USA
关键词
D O I
10.1104/pp.116.2.859
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Choline monooxygenase (CMO) catalyzes the committing step in the synthesis of glycine betaine, an osmoprotectant accumulated by many plants in response to salinity and drought. To investigate how these stresses affect CMO expression, a spinach (Spinacia oleracea L., Chenopodiaceae) probe was used to isolate CMO cDNAs from sugar beet (Beta vulgaris L., Chenopodiaceae), a salt- and drought-tolerant crop. The deduced beet CMO amino acid sequence comprised a transit peptide and a 381-residue mature peptide that was 84% identical (97% similar) to that of spinach and that showed the same consensus motif for coordinating a Rieske-type [2Fe-2S] cluster. A mononuclear Fe-binding motif was also present. When water was withheld, leaf relative water content declined to 59% and the levels of CMO mRNA, protein, and enzyme activity rose 3- to 5-fold; rewatering reversed these changes. After gradual salinization (NaCl:CaCl2 = 5.7:1, mol/mol), CMO mRNA, protein, and enzyme levels in leaves increased 3- to 7-fold at 400 mM salt, and returned to uninduced levels when salt was removed. Beet roots also expressed CMO, most strongly when salinized. Salt-inducible CMO mRNA, protein, and enzyme activity were readily detected in leaves of Amaranthus caudatus L. (Amaranthaceae). These data show that CMO most probably has a mononuclear Fe center, is inducibly expressed in roots as well as in leaves of Chenopodiaceae, and is not unique to this family.
引用
收藏
页码:859 / 865
页数:7
相关论文
共 41 条
[31]   Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: Prosthetic group characterization and cDNA cloning [J].
Rathinasabapathi, B ;
Burnet, M ;
Russell, BL ;
Gage, DA ;
Liao, PC ;
Nye, GJ ;
Scott, P ;
Golbeck, JH ;
Hanson, AD .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (07) :3454-3458
[32]  
RATHINASABAPATHI B, 1994, PLANTA, V193, P155, DOI 10.1007/BF00192524
[33]   DETERMINATION OF BETAINES BY FAST-ATOM-BOMBARDMENT MASS-SPECTROMETRY - IDENTIFICATION OF GLYCINE BETAINE DEFICIENT GENOTYPES OF ZEA-MAYS [J].
RHODES, D ;
RICH, PJ ;
MYERS, AC ;
REUTER, CC ;
JAMIESON, GC .
PLANT PHYSIOLOGY, 1987, 84 (03) :781-788
[34]  
RHODES D, 1993, ANNU REV PLANT PHYS, V44, P357, DOI 10.1146/annurev.pp.44.060193.002041
[35]  
Rydzik E, 1996, PLANT PHYSIOL, V110, P713
[36]   ISOLATION AND PRELIMINARY CHARACTERIZATION OF THE SUBUNITS OF THE TERMINAL COMPONENT OF NAPHTHALENE DIOXYGENASE FROM PSEUDOMONAS-PUTIDA NCIB 9816-4 [J].
SUEN, WC ;
GIBSON, DT .
JOURNAL OF BACTERIOLOGY, 1993, 175 (18) :5877-5881
[37]  
Takhtajan A., 1969, FLOWERING PLANTS ORI
[38]   PHYTOCHROME IN GREEN TISSUE - SPECTRAL AND IMMUNOCHEMICAL EVIDENCE FOR 2 DISTINCT MOLECULAR-SPECIES OF PHYTOCHROME IN LIGHT-GROWN AVENA-SATIVA L [J].
TOKUHISA, JG ;
DANIELS, SM ;
QUAIL, PH .
PLANTA, 1985, 164 (03) :321-332
[39]  
VALENZUELASOTO EM, 1993, J BIOL CHEM, V268, P23818
[40]   Betaine aldehyde dehydrogenase in sorghum - Molecular cloning and expression of two related genes [J].
Wood, AJ ;
Saneoka, H ;
Rhodes, D ;
Joly, RJ ;
Goldsbrough, PB .
PLANT PHYSIOLOGY, 1996, 110 (04) :1301-1308