+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Inhibitory serpins from wheat grain with reactive centers resembling glutamine-rich repeats of prolamin storage proteins. Cloning and characterization of five major molecular forms



Inhibitory serpins from wheat grain with reactive centers resembling glutamine-rich repeats of prolamin storage proteins. Cloning and characterization of five major molecular forms



Journal of Biological Chemistry 275(43): 33272



Genes encoding proteins of the serpin superfamily are widespread in the plant kingdom, but the properties of very few plant serpins have been studied, and physiological functions have not been elucidated. Six distinct serpins have been identified in grains of hexaploid bread wheat (Triticum aestivum L.) by partial purification and amino acid sequencing. The reactive centers of all but one of the serpins resemble the glutamine-rich repetitive sequences in prolamin storage proteins of wheat grain. Five of the serpins, classified into two protein Z subfamilies, WSZ1 and WSZ2, have been cloned, expressed in Escherichia coli, and purified. Inhibitory specificity toward 17 proteinases of mammalian, plant, and microbial origin was studied. All five serpins were suicide substrate inhibitors of chymotrypsin and cathepsin G. WSZ1a and WSZ1b inhibited at the unusual reactive center P(1)-P(1)' Gln-Gln, and WSZ2b at P(2)-P(1) Leu-Arg-one of two overlapping reactive centers. WSZ1c with P(1)-P(1)' Leu-Gln was the fastest inhibitor of chymotrypsin (k(a) = 1.3 x 10(6) m(-1) s(-1)). WSZ1a was as efficient an inhibitor of chymotrypsin as WSZ2a (k(a) approximately 10(5) m(-1) s(-1)), which has P(1)-P(1)' Leu-Ser-a reactive center common in animal serpins. WSZ2b inhibited plasmin at P(1)-P(1)' Arg-Gln (k(a) approximately 10(3) m(-1) s(-1)). None of the five serpins inhibited Bacillus subtilisin A, Fusarium trypsin, or two subtilisin-like plant serine proteinases, hordolisin from barley green malt and cucumisin D from honeydew melon. Possible functions involving interactions with endogenous or exogenous proteinases adapted to prolamin degradation are discussed.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 010853729

Download citation: RISBibTeXText

PMID: 10874043

DOI: 10.1074/jbc.m004633200


Related references

Inhibitory serpins from rye grain with glutamine as P1 and P2 residues in the reactive center. FEBS Letters 488(3): 149-153, 2001

Molecular cloning and characterization of a cysteine-rich 16.6-kDa prolamin in rice seeds. Bioscience Biotechnology and Biochemistry 63(11): 1851-1858, 1999

Serpins in fruit and vegetative tissues of apple (Malus domestica): expression of four serpins with distinct reactive centres and characterisation of a major inhibitory seed form, MdZ1b. Functional Plant Biology 32(6): 517-527, 2005

Glutamine Repeats and Neurodegenerative Diseases: Molecular Aspects || Aggregation of Truncated GST-HD Exon 1 Fusion Proteins Containing Normal Range and Expanded Glutamine Repeats. Philosophical Transactions Biological Sciences 354(1386): 991-994, 1999

Inhibitory plant serpins with a sequence of three glutamine residues in the reactive center. Biological Chemistry 386(12): 1319-1323, 2005

Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid b-peptide of amyloid plaques. Proceedings of the National Academy of Sciences of the United States of America 99(8): 96-600, 2002

Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques. Proceedings of the National Academy of Sciences of the United States of America 99(8): 5596-5600, 2002

The purification and characterization of homologous high molecular weight storage proteins from grain of wheat, rye and barley. Tag. Theoretical and Applied Genetics. Theoretische und Angewandte Genetik 62(4): 329-336, 1982

Seed Storage Proteins || The Structural and Evolutionary Relationships of the Prolamin Storage Proteins of Barley, Rye and Wheat. Philosophical Transactions of the Royal Society of London Series B Biological Sciences 304(1120): 297-308, 1984

Serpins of oat (Avena sativa) grain with distinct reactive centres and inhibitory specificity. Physiologia Plantarum 116(2): 155-163, 2002

The prolamin storage proteins of wheat and its relatives. Cellular and molecular biology of plant seed development 256, 1997

The prolamin storage proteins of wheat and related cereals. Progress in Biophysics and Molecular Biology 61(1): 37-59, 1994

Contribution to the study of albumin and prolamin contents in the grain of newly bred forms of winter wheat. Vedecke Prace Vyskumneho Ustavu Rastlinnej Vyroby v Piest' anoch, Obilniny i Strukoviny 21: 91-98, 1986

Molecular characterization of glutamic acid/glutamine-rich secretory proteins from rat submandibular glands. Journal of Biological Chemistry 262(15): 7289-7297, 1987

The structural and evolutionary relationships of the prolamin storage proteins of barley, rye and wheat. Philosophical Transactions of the Royal Society of London, B Biological Sciences 304(1120): 297-308, 1984