Cloning and expression of a new cDNA from monocotyledonous plants coding for a diadenosine 5′,5′′′‐P1,P4‐tetraphosphate hydrolase from barley (Hordeum vulgare)

• Published in: FEBS letters 1998-07, Vol.431 (3), p.481-485
• Main Authors: Churin, Juri, Hause, Bettina, Feussner, Ivo, Maucher, Helmut P, Feussner, Kirstin, Börner, Thomas, Wasternack, Claus
• Format: Article
• Language: English
• Subjects: Acid Anhydride Hydrolases - genetics; Acid Anhydride Hydrolases - metabolism; Amino Acid Sequence; Base Sequence; Cloning, Molecular; Cloning, overexpression; Diadenosine 5′,5′′′-P1,P4-tetraphosphate (Ap4A) hydrolase; DNA, Complementary; Hordeum - enzymology; Hordeum - genetics; Hordeum vulgare; Humans; Molecular Sequence Data; Sequence Homology, Amino Acid
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(98)00819-9

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′′′‐P1,P4‐tetraphosphate (Ap4A) hydrolase of Lupinus angustifolius (Maksel et al. (1998) Biochem. J. 329, 313–319), and 69% identity to four partial peptide sequences of Ap4A hydrolase of tomato. Overexpression in Escherichia coli revealed a protein of about 19 kDa, which exhibited Ap4A hydrolase activity and cross‐reactivity with an antibody raised against a purified tomato Ap4A 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 Ap4A hydrolase in plants will be discussed.