EurekaMag.com logo
+ Site Statistics
References:
53,214,146
Abstracts:
29,074,682
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Systemically wound-responsive genes in poplar trees encode proteins similar to sweet potato sporamins and legume Kunitz trypsin inhibitors






Plant molecular biology: an international journal on molecular biology biochemistry and genetic engineering 14(1): 51-59

Systemically wound-responsive genes in poplar trees encode proteins similar to sweet potato sporamins and legume Kunitz trypsin inhibitors

When the lower leaves of hybrid poplar trees are mechanically wounded, several novel mRNAs accumulate in the unwounded upper leaves (Parsons TJ, Bradshaw HD, Gordon MP: Systemic accumulation of specific mRNAs in response to wounding in poplar trees, Proc Natl Acad Sci USA, in press). A partial cDNA clone corresponding to a transcript from the wound-responsive gene designated win 3 (wound-inducible) has been cloned by differential hybridization to 32P-labelled cDNA from the leaves of wounded trees. Northern blots show a large accumulation of win 3 transcripts in the unwounded leaves of wounded trees. Southern blot analysis of poplar DNA suggests that win 3 is a member of a multigene family. The nucleotide sequences of several win 3 cDNA clones have been determined, indicating that at least three win 3 gene family members are transcribed. A genomic clone of a win 3 gene family member has been isolated and a 1.5 kb Hind III fragment containing the predicted protein-coding and 5' upstream regions has been sequenced. The putative win 3 gene product is similar to the major soluble proteins of sweet potato tubers, sporamin A and sporamin B. Both Win3 and the sporamins share significant amino acid sequence identity with Kunitz-type trypsin inhibitors from legume seeds. The Kunitz family of proteinase inhibitors thus joints three other proteinase inhibitor families which are systemically responsive to wounding.

Accession: 001962901

PMID: 2101311

DOI: 10.1007/bf00015654

Download PDF Full Text: Systemically wound-responsive genes in poplar trees encode proteins similar to sweet potato sporamins and legume Kunitz trypsin inhibitors



Related references

A family of potato genes that encode Kunitz-type proteinase inhibitors: structural comparisons and differential expression. Plant & Cell Physiology 35(2): 303-312, 1994

Method for the elimination of Kunitz and Bowman-Birk trypsin inhibitors and carboxypeptidase inhibitor from potato proteins. Official Gazette of the United States Patent & Trademark Office Patents 1279(1), Feb 3, 2004

Proteinase inhibitors from a mimosoideae legume, Albizzia julibrissin. Homologues of soybean trypsin inhibitor (Kunitz). Journal of Biochemistry 86(6): 1795-1805, 1979

Sweet potato Lam trypsin inhibitors, the major root storage proteins, inhibit one endogenous serine protease activity. Plant Science (Oxford) 163(4): 733-739, October, 2002

An aspartic type protease degrades trypsin inhibitors, the major root storage proteins of sweet potato Lam cv Tainong 57. Botanical Bulletin of Academia Sinica (Taipei) 43(4): 271-276, October, 2002

Molecular evolution of a small gene family of wound inducible Kunitz trypsin inhibitors in Populus. Journal of Molecular Evolution 63(1): 108-119, 2006

N-terminal amino acid sequence of trypsin inhibitor 3 from winged bean Psophocarpus tetragonolobus, relationship to other legume Kunitz-type inhibitors. Phytochemistry 2(3): 767-768, 1983

Sweet potato (Ipomoea batatas (L.) Lam) trypsin inhibitors, the major root storage proteins, inhibit one endogenous serine protease activity. Plant Science 163(4): 733-739, 2002

An aspartic type protease degrades trypsin inhibitors, the major root storage proteins of sweet potato (Ipomoea batatas (L.) Lam cv. Tainong 57). Botanical Bulletin of Academia Sinica 43(4): 271-276, 2002

Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, X. The amino-acid sequences of the trypsin-released inhibitors from horse and pig inter-alpha-trypsin inhibitors. Biological Chemistry Hoppe-Seyler 366(5): 473-478, 1985