Seed storage globulins: Origin and evolution of primary and higher order structures

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• 作者：A. S. Rudakova ; A. M. Cherdivar? ; K. A. Wilson ; A. D. Shutov
• 关键词：seed storage globulins ; germins ; oxalate decarboxylases ; tertiary structure ; evolution ; proteolysis
• 刊名：Biochemistry (Moscow)
• 出版年：2015
• 出版时间：October 2015
• 年：2015
• 卷：80
• 期：10
• 页码：1354-1361
• 全文大小：950 KB
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  12.Shutov, A. D., and Wilson, K. A. (2014) Seed storage glob-ulins: their descent from bacterial ancestors and mecha-nisms of degradation, in Globulins: Biochemistry, Production and Role in Immunity (Milford, S. D., ed.) Nova Science Publishers, New York, pp. 71-04.
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  14.Shutov, A. D., and Baumlein, H. (1999) Origin and evolu-tion of seed storage globulins (Shewry, P. R., and Casey, R., eds.) Kluwer Academic Publishers, Dordrecht, pp. 543-61.
  15.Shutov, A. D., Braun H., Chesnokov, Yu. V., and Baumlein, H. (1998) A gene encoding a vicilin-like protein is specifi-cally expressed in fern spores. Evolutionary pathway of seed storage globulins, Eur. J. Biochem., 252, 79-9.CrossRef PubMed
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• 作者单位：A. S. Rudakova (1)
  A. M. Cherdivar? (1)
  K. A. Wilson (2)
  A. D. Shutov (1)
  
  1. State University of Moldova, Kishinev, MD, 2009, Moldova
  2. State University of New York at Binghamton, Binghamton, NY, 13902-6000, USA
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Bioorganic Chemistry
  Microbiology
  Biomedicine
  Russian Library of Science
  
• 出版者：MAIK Nauka/Interperiodica distributed exclusively by Springer Science+Business Media LLC.
• ISSN：1608-3040

文摘

Legumin and vicilin are two-domain seed storage globulins similar in primary and higher order structures of their domains to single-domain plant germins as well as to the domains of two-domain and single-domain bacterial oxalate decarboxylases. Independent evolutionary pathways have been shown for the descent of the storage globulins and germins from two-domain and single-domain bacterial oxalate decarboxylases, respectively. As compared to vicilins, the primary and tertiary structures of legumins were found to most closely reflect the ancient features characteristic of a common precursor of storage globulins. During the evolution of the storage globulins, a mechanism specifically controlling their degradation has been formed. We found that limited proteolysis of soybean legumin and kidney bean vicilin in germinating seeds and in vitro leads to their regular changes, which initiate an extensive cleavage of storage globulin molecules by the one-by-one mechanism. As also shown, limited proteolysis of soybean legumin loosens the intersubunit interactions in its oligomeric molecule. Based on these data, we hypothesize that the deep one-by-one degradation of soybean legumin is triggered by its dissociation, which bares peptide bonds potentially susceptible to proteolytic attack but are masked in the oligomer. Keywords seed storage globulins germins oxalate decarboxylases tertiary structure evolution proteolysis