L. Bremaud et al., TRANSLATION INITIATION-FACTOR IF2 OF THE MYXOBACTERIUM STIGMATELLA-AURANTIACA - PRESENCE OF A SINGLE-SPECIES WITH AN UNUSUAL N-TERMINAL SEQUENCE, Journal of bacteriology, 179(7), 1997, pp. 2348-2355
The structural gene for translation initiation factor IF2 (infB) was i
solated from the myxobacterium Stigmatella aurantiaca on a 5.18-kb Bam
HI genomic restriction fragment. The infB gene (ca. 3.16 kb) encodes a
1,054-residue polypeptide with extensive homology within its G domain
and C terminus with the equivalent regions of IF2s from Escherichia c
oli, Bacillus subtilis, Bacillus stearothermophilus, and Streptococcus
faecium. The N-terminal region does not display any significant homol
ogy to other known proteins. The S. aurantiaca infB gene encodes a sin
gle protein which cross-reacted with antiserum to E. coli IF2 and was
able to complement an E. coli infB mutant. The S. aurantiaca IF2 is di
stinguished from all other IF2s by a sequence of 160 residues near the
N terminus that has an unusual composition, made up essentially of al
anine, proline, valine, and glutamic acid. Within this sequence, the p
attern PXXXAP is repeated nine times. Complete deletion of this sequen
ce did not affect the factor's function in initiation of translation a
nd even increased its capacity to complement the E. coli infB mutant.