Deaggregation of eIF4E induced by mRNA 5' cap binding.
All eukaryotic mRNAs contain a 5' terminal cap structure, which consists of 7-methylguanosine linked by a 5-5' triphosphate bridge to the first transcribed nucleoside (m7GpppN). Specific recognition of the cap by the eukaryotic initiation factor eIF4E plays a key role in regulation of translation initiation as a rate-limiting step. Using dynamic light scattering (DLS), the apo-form of murine eIF4E (33-217) was shown to aggregate. After addition of m7G7P, progressive deaggregation with the time of incubation in the presence of the cap analogue has been observed.
Niedzwiecka
Anna
A
Department of Biophysics, Institute of Experimental Physics, Warsaw University, Warsaw, Poland. annan@ifpan.edu.pl
Darzynkiewicz
Edward
E
Stolarski
Ryszard
R
D000818:Animals; D004926:Escherichia coli / Q000378:metabolism; D039561:Eukaryotic Initiation Factor-4E / Q000737:chemistry*; D007700:Kinetics; D008027:Light; D046911:Macromolecular Substances; D051379:Mice; D008956:Models, Chemical; D010448:Peptide Initiation Factors / Q000737:chemistry; D010710:Phosphates / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011522:Protons; D012314:RNA Cap Analogs / Q000737:chemistry; D012315:RNA Caps; D012333:RNA, Messenger / Q000378:metabolism*; D012542:Scattering, Radiation; D013997:Time Factors
D039561:Eukaryotic Initiation Factor-4E; D046911:Macromolecular Substances; D010448:Peptide Initiation Factors; D010710:Phosphates; D011522:Protons; D012314:RNA Cap Analogs; D012315:RNA Caps; D012333:RNA, Messenger