PMID- 22367534
OWN - NLM
STAT- MEDLINE
DCOM- 20140122
LR  - 20211021
IS  - 1615-6102 (Electronic)
IS  - 0033-183X (Linking)
VI  - 250
IP  - 1
DP  - 2013 Feb
TI  - Oligomerization of the reversibly glycosylated polypeptide: its role during rice 
      plant development and in the regulation of self-glycosylation.
PG  - 111-9
LID - 10.1007/s00709-012-0382-x [doi]
AB  - 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      cluster analysis and secondary structure prediction revealed that class 2 RGPs no 
      longer maintained the Rossman fold described for class 1 RGP.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.
FAU - De Pino, Veronica
AU  - De Pino V
AD  - Facultad de Farmacia y Bioquimica, Catedra de Farmacognosia, INQUIMEFA-Consejo 
      Nacional de Investigaciones Cientificas y Tecnicas, Junin 954, Ciudad Autonoma de 
      Buenos Aires (1113), Argentina.
FAU - Marino Busjle, Cristina
AU  - Marino Busjle C
FAU - Moreno, Silvia
AU  - Moreno S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20120225
PL  - Austria
TA  - Protoplasma
JT  - Protoplasma
JID - 9806853
RN  - 0 (Peptides)
RN  - 0 (Plant Proteins)
SB  - IM
MH  - Glycosylation
MH  - Oryza/genetics/growth & development/*metabolism
MH  - Peptides/genetics/*metabolism
MH  - Plant Development
MH  - Plant Proteins/genetics/*metabolism
EDAT- 2012/03/01 06:00
MHDA- 2014/01/23 06:00
CRDT- 2012/02/28 06:00
PHST- 2011/12/05 00:00 [received]
PHST- 2012/01/23 00:00 [accepted]
PHST- 2012/02/28 06:00 [entrez]
PHST- 2012/03/01 06:00 [pubmed]
PHST- 2014/01/23 06:00 [medline]
AID - 10.1007/s00709-012-0382-x [doi]
PST - ppublish
SO  - Protoplasma. 2013 Feb;250(1):111-9. doi: 10.1007/s00709-012-0382-x. Epub 2012 Feb 
      25.