PMID- 18211834
OWN - NLM
STAT- MEDLINE
DCOM- 20080522
LR  - 20161126
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1779
IP  - 3
DP  - 2008 Mar
TI  - Prior interaction of ATP with yeast mRNAs enhances protein synthesis at the 
      initiation step.
PG  - 175-82
LID - 10.1016/j.bbagrm.2007.12.009 [doi]
AB  - ATP hydrolysis is important for different stages of the protein synthesis 
      process. A novel effect of this nucleotide was detected using mRNAs isolated from 
      S. cerevisiae after phenol extraction of polysomes. When polysomal mRNA (pmRNA) 
      or poly(A)(+) RNA were preincubated with ATP (approximately 3 mM, near 
      physiological concentration), their translational activity in a cell-free system 
      from yeast was stimulated 2-3 fold. This increased translational activity is 
      specific for the poly(A)(+) RNA fraction, correlates with facilitated assembly of 
      80S initiation complexes, and is associated to increased synthesis of high 
      molecular weight polypeptides. TCA precipitation assays of RNA incubated with 
      [(14)C]ATP suggested an association of the nucleotide with the nucleic acid. The 
      amount of [(14)C]ATP co-precipitated was dependent on magnesium (optimum at 5-6 
      mM), was partially inhibited by monovalent ions, and was maximal with poli(A)(+) 
      RNA. Existence of RNA-associated kinases or ATPases appear unlikely since neither 
      phosphorylation nor nucleotide hydrolysis were observed during preincubation of 
      pmRNA with ATP. Another evidence of ATP-RNA interaction was an increased 
      absorbance at 260 nm after incubation suggesting unwinding of the RNA secondary 
      structure. Therefore, preincubation with ATP may affect the conformation of mRNAs 
      and thereby facilitate the initiation of protein synthesis. This event could be 
      part of an in vivo energy-dependent mechanism for translational control.
FAU - Triana, Juana Ledia
AU  - Triana JL
AD  - Instituto de Investigaciones Biomedicas , Facultad de Ciencias de la Salud, 
      Universidad de Carabobo, Sede Aragua, Venezuela.
FAU - Mendez, Yda
AU  - Mendez Y
FAU - Navarro, Luis
AU  - Navarro L
FAU - Reggio, Ronald
AU  - Reggio R
FAU - Ferreras, Ana Celia
AU  - Ferreras AC
FAU - Edmundo, Cayama
AU  - Edmundo C
FAU - Triana-Alonso, Francisco J
AU  - Triana-Alonso FJ
FAU - Herrera, Flor
AU  - Herrera F
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20080103
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (RNA, Messenger)
RN  - 24937-83-5 (Poly A)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
SB  - IM
MH  - Adenosine Triphosphate/*physiology
MH  - *Peptide Chain Initiation, Translational
MH  - Poly A/metabolism
MH  - *Protein Biosynthesis
MH  - RNA, Messenger/*physiology
MH  - Saccharomyces cerevisiae/*genetics
EDAT- 2008/01/24 09:00
MHDA- 2008/05/23 09:00
CRDT- 2008/01/24 09:00
PHST- 2007/05/08 00:00 [received]
PHST- 2007/12/07 00:00 [revised]
PHST- 2007/12/27 00:00 [accepted]
PHST- 2008/01/24 09:00 [pubmed]
PHST- 2008/05/23 09:00 [medline]
PHST- 2008/01/24 09:00 [entrez]
AID - S1874-9399(07)00202-7 [pii]
AID - 10.1016/j.bbagrm.2007.12.009 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2008 Mar;1779(3):175-82. doi: 10.1016/j.bbagrm.2007.12.009. 
      Epub 2008 Jan 3.