PMID- 23002146
OWN - NLM
STAT- MEDLINE
DCOM- 20130130
LR  - 20211021
IS  - 1362-4962 (Electronic)
IS  - 0305-1048 (Print)
IS  - 0305-1048 (Linking)
VI  - 40
IP  - 21
DP  - 2012 Nov
TI  - Rbg1-Tma46 dimer structure reveals new functional domains and their role in 
      polysome recruitment.
PG  - 11100-14
LID - 10.1093/nar/gks867 [doi]
AB  - Developmentally Regulated GTP-binding (DRG) proteins are highly conserved GTPases 
      that associate with DRG Family Regulatory Proteins (DFRP). The resulting 
      complexes have recently been shown to participate in eukaryotic translation. The 
      structure of the Rbg1 GTPase, a yeast DRG protein, in complex with the C-terminal 
      region of its DFRP partner, Tma46, was solved by X-ray diffraction. These data 
      reveal that DRG proteins are multimodular factors with three additional domains, 
      helix-turn-helix (HTH), S5D2L and TGS, packing against the GTPase platform. 
      Surprisingly, the S5D2L domain is inserted in the middle of the GTPase sequence. 
      In contrast, the region of Tma46 interacting with Rbg1 adopts an extended 
      conformation typical of intrinsically unstructured proteins and contacts the 
      GTPase and TGS domains. Functional analyses demonstrate that the various domains 
      of Rbg1, as well as Tma46, modulate the GTPase activity of Rbg1 and contribute to 
      the function of these proteins in vivo. Dissecting the role of the different 
      domains revealed that the Rbg1 TGS domain is essential for the recruitment of 
      this factor in polysomes, supporting further the implication of these conserved 
      factors in translation.
FAU - Francis, Sandrea M
AU  - Francis SM
AD  - Instituto de Biomedicina de Valencia (IBV-CSIC), Calle Jaime Roig, 11, Valencia 
      E-46010, Spain.
FAU - Gas, Maria-Eugenia
AU  - Gas ME
FAU - Daugeron, Marie-Claire
AU  - Daugeron MC
FAU - Bravo, Jeronimo
AU  - Bravo J
FAU - Seraphin, Bertrand
AU  - Seraphin B
LA  - eng
SI  - PDB/4A9A
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20120923
PL  - England
TA  - Nucleic Acids Res
JT  - Nucleic acids research
JID - 0411011
RN  - 0 (Fungal Proteins)
RN  - 149371-72-2 (developmentally regulated GTP-binding protein)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Dimerization
MH  - Fungal Proteins/*chemistry/genetics/metabolism
MH  - GTP-Binding Proteins/*chemistry/metabolism
MH  - Gene Deletion
MH  - Guanosine Triphosphate/metabolism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Polyribosomes/*metabolism
MH  - Protein Structure, Tertiary
MH  - Static Electricity
PMC - PMC3510508
EDAT- 2012/09/25 06:00
MHDA- 2013/01/31 06:00
PMCR- 2012/09/23
CRDT- 2012/09/25 06:00
PHST- 2012/09/25 06:00 [entrez]
PHST- 2012/09/25 06:00 [pubmed]
PHST- 2013/01/31 06:00 [medline]
PHST- 2012/09/23 00:00 [pmc-release]
AID - gks867 [pii]
AID - 10.1093/nar/gks867 [doi]
PST - ppublish
SO  - Nucleic Acids Res. 2012 Nov;40(21):11100-14. doi: 10.1093/nar/gks867. Epub 2012 
      Sep 23.