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J. Biol. Chem., Vol. 277, Issue 38, 35541-35549, September 20, 2002
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From the Department of Chemistry, University of North Carolina,
Chapel Hill, North Carolina 27599-3290
Human mitochondrial translational initiation
factor 3 (IF3mt) has been identified from the human
expressed sequence tag data base. Using consensus sequences
derived from conserved regions of the bacterial IF3, several partially
sequenced cDNA clones were identified, and the complete sequence
was assembled in silico from overlapping clones.
IF3mt is 278 amino acid residues in length. MitoProt II
predicts a 97% probability that this protein will be localized in
mitochondria and further predicts that the mature protein will be 247 residues in length. The cDNA for the predicted mature form of
IF3mt was cloned, and the protein was expressed in
Escherichia coli in a His-tagged form. The mature form of
IF3mt has short extensions on the N and C termini
surrounding a region homologous to bacterial IF3. The region of
IF3mt homologous to prokaryotic factors ranges between
21-26% identical to the bacterial proteins. Purified
IF3mt promotes initiation complex formation on
mitochondrial 55 S ribosomes in the presence of mitochondrial initiation factor 2 (IF2mt), [35S]fMet-tRNA,
and either poly(A,U,G) or an in vitro transcript of the
cytochrome oxidase subunit II gene as mRNA. IF3mt
shifts the equilibrium between the 55 S mitochondrial ribosome and its subunits toward subunit dissociation. In addition, the ability of
E. coli initiation factor 1 to stimulate initiation complex formation on E. coli 70 S and mitochondrial 55 S ribosomes
was investigated in the presence of IF2mt and
IF3mt.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF410851 and AAL04150.
Identification of Mammalian Mitochondrial Translational
Initiation Factor 3 and Examination of Its Role in Initiation Complex
Formation with Natural mRNAs*
*
This work was supported by National Institutes of Health
Grant GM32734.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
919-966-1567; Fax: 919-966-3675; E-mail:
Linda_Spremulli@unc.edu.
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