Abstract
From a cDNA library generated from mRNA of white leaf tissues of the ribosome-deficient mutant `albostrians' of barley ( Hordeum vulgare cv. Haisa) a cDNA was isolated carrying 54.2% identity to a recently published cDNA which codes for the diadenosine-5′,5′′′-P 1,P 4-tetraphosphate (Ap 4A) hydrolase of Lupinus angustifolius (Maksel et al. (1998) Biochem. J. 329, 313–319), and 69% identity to four partial peptide sequences of Ap 4A hydrolase of tomato. Overexpression in Escherichia coli revealed a protein of about 19 kDa, which exhibited Ap 4A hydrolase activity and cross-reactivity with an antibody raised against a purified tomato Ap 4A hydrolase (Feussner et al. (1996) Z. Naturforsch. 51c, 477–486). Expression studies showed an mRNA accumulation in all organs of a barley seedling. Possible functions of Ap 4A hydrolase in plants will be discussed.
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