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PLANT PHYSIOLOGY , Vol 101, Issue 2 667-674, Copyright © 1993 by American Society of Plant Biologists

MOLECULAR BIOLOGY AND GENE REGULATION

Protein Farnesyltransferase in Plants (Molecular Cloning and Expression of a Homolog of the [beta] Subunit from the Garden Pea)

Z. Yang, C. L. Cramer and J. C. Watson
Department of Botany (Z.Y.) and Maryland Agricultural Experiment Station and Center for Agricultural Biotechnology (J.C.W.), University of Maryland, College Park, Maryland 20742-5815

Protein farnesyltransferase is a heterodimeric enzyme that attaches a farnesyl moiety to C-terminal cysteine residues. Both the [alpha] and [beta] subunits have recently been cloned and sequenced from yeast and rat. Degenerate oligonucleotides, corresponding to conserved regions of the [beta] subunit, were used as primers for the polymerase chain reaction to amplify cDNA synthesized from total cellular RNA from the apical buds of pea (Pisum sativum L.) seedlings. The 171-bp fragment obtained encodes an open reading frame of 57 amino acids showing 65% identity to the rat protein farnesyltransferase [beta] subunit. Using this fragment to screen a pea cDNA library, one full-length cDNA clone, designated PsFTb, was obtained that contains an open reading frame encoding a polypeptide of 419 amino acids. The predicted amino acid sequence exhibits 48 and 40% identity to the rat and yeast [beta] subunits, respectively, indicating that this cDNA encodes a pea homolog of the [beta] subunit of farnesyltransferase. Gel blot hybridizations show that PsFTb is likely to be encoded by a single-copy gene and is expressed as a transcript of approximately 1.7 kb. During photo-regulated leaf development in continuous white light, PsFTb transcript levels within apical buds decline by approximately 5-fold.


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