Microbial relatives of seed storage proteins: Conservation of motifs in a functionally diverse superfamily of enzymes

被引:61
作者
Dunwell, JM
Gane, PJ
机构
[1] Univ Reading, Sch Plant Sci, Dept Agr Bot, Reading RG6 6AS, Berks, England
[2] Inst Food Res, Reading Lab, Reading RG6 6BZ, Berks, England
关键词
seed storage proteins; enzyme superfamily; protein domain; germin; oxalate oxidase; histidine cluster; mannose metabolism;
D O I
10.1007/PL00006289
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Plant storage proteins comprise a major part of the human diet. Sequence analysis has revealed that these proteins probably share a common ancestor with a fungal oxalate decarboxylase and/or related bacterial genes. Additionally, all these proteins share a central core sequence with several other functionally diverse enzymes and binding proteins, many of which are associated with synthesis of the extracellular matrix during sporulation/encystment. A possible prokaryotic relative of this sequence is a bacterial protein (SASP) known to bind to DNA and thereby protect spores from extreme environmental conditions. This ability to maintain cell viability during periods of dehydration in spores and seeds may relate to absolute conservation of residues involved in structure determination.
引用
收藏
页码:147 / 154
页数:8
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