NDLI: Oligomerization of the reversibly glycosylated polypeptide: its role during rice plant development and in the regulation of self-glycosylation

Content Provider	Springer Nature Link
Author	De Pi, Verónica Mari Busjle, Cristina More, Silvia
Copyright Year	2012
Abstract	A multigenic family of self-glycosylating proteins named reversibly glycosylated polypeptides, designated as RGPs, have been usually associated with carbohydrate metabolism, although they are an enigma both at the functional, as well as at the structural level. In this work, we used biochemical approaches to demonstrate that complex formation is linked to rice plant development, in which class 1 Oryza sativa RGP (OsRGP) would be involved in an early stage of growing plants, while class 2 OsRGP would be associated with a late stage linked to an active polysaccharide synthesis that occurs during the elongation of plant. Here, a further investigation of the complex formation of the Solanum tuberosum RGP (StRGP) was performed. Results showed that disulfide bonds are at least partially responsible for maintaining the oligomeric protein structure, so that the nonreduced StRGP protein showed an apparent higher molecular weight and a lower radioglycosylation of the monomer with respect to its reduced form. Hydrophobic cluster analysis and secondary structure prediction revealed that class 2 RGPs no longer maintained the Rossman fold described for class 1 RGP. A 3D structure of the StRGP protein resolved by homology modeling supports the possibility of intercatenary disulfide bridges formed by exposed cysteines residues C79, C303 and C251 and they are most probably involved in complex formation occurring into the cell cytoplasm.
Starting Page	111
Ending Page	119
Page Count	9
File Format	PDF
ISSN	0033183X
Journal	Protoplasma
Volume Number	250
Issue Number	1
e-ISSN	16156102
Language	English
Publisher	Springer Vienna
Publisher Date	2012-02-25
Publisher Place	Vienna
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Complex formation Plant polysaccharide Self-glycosylation Reversibly glycosylated polypeptide Cell Biology Plant Sciences Zoology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Plant Science Medicine

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