Plant Physiol. Illumina
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Plant Physiology 78:285-290 (1985)
© 1985 American Society of Plant Biologists

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Articles

Subcellular and Developmental Distribution of {beta}-Cyanoalanine Synthase in Barley Leaves 1

Eve Syrkin Wurtele2, Basil J. Nikolau3 and Eric E. Conn

Department of Biochemistry and Biophysics, University of California, Davis, California 95616

The subcellular and developmental distribution of {beta}-cyanoalanine synthase (EC 4.4.1.9), which catalyzes the reaction between cysteine and HCN to form {beta}-cyanoalanine and H2S, were investigated in barley (Hordeum vulgare) leaves. Total leaf activity was 1.1 micromoles per minute per gram fresh weight. Sucrose density gradients of lysed mesophyll protoplasts of barley revealed the exclusive or predominant localization of {beta}-cyanoalanine synthase in the mitochondria. The enzyme was absent from both vacuole and chloroplast fractions.

{beta}-Cyanoalanine synthase activity was distributed over the entire length of the barley leaf. Activity was dependent on the developmental stage, with a 3.5-fold higher activity in the oldest (apical) compared to the youngest (basal) parts of the leaf. The corresponding difference in activity for mesophyll protoplasts isolated from these parts was 7.5-fold. In younger leaf seagments, the nonchlorophyllous tissues accounted for up to 70% of the total {beta}-cyanoalanine synthase activity. These results are discussed with reference to the formation of HCN as a substrate in barley leaves.


2 Present address: NPI, 417 Wakara Way, Salt Lake City, UT 84108.

3 Present address: Department of Cellular, Viral, and Molecular Biology, University of Utah, Salt Lake City, UT 84132.

1 Supported in part by National Science Foundation Grants PCM-81-04497 and PCM79-03976 and by United States Public Health Service Grant GM-05301-25.




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