Characterization of Bacillus stearothermophilus infA and of its product IF1

• Published in: Gene 2009, Vol.428 (1), p.31-35
• Main Authors: Kapralou, Stavroula, Fabbretti, Attilio, Garulli, Chiara, Gualerzi, Claudio O., Pon, Cynthia L., Spurio, Roberto
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Bacillus stearothermophilus; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Base Sequence; Blotting, Northern; Blotting, Western; Escherichia coli; Escherichia coli - genetics; Escherichia coli - metabolism; Eukaryotic Initiation Factor-1 - genetics; Eukaryotic Initiation Factor-1 - metabolism; Geobacillus stearothermophilus - genetics; Geobacillus stearothermophilus - metabolism; Molecular Sequence Data; Peptide Chain Initiation, Translational; Prokaryotic Initiation Factor-1 - genetics; Prokaryotic Initiation Factor-1 - metabolism; Protein synthesis; Reverse Transcriptase Polymerase Chain Reaction; Ribosomes; RNA, Bacterial - genetics; RNA, Bacterial - metabolism; RNA, Messenger - genetics; RNA, Messenger - metabolism; Sequence Homology, Amino Acid; Thermophilic IF1; Translation initiation in Gram positives
• ISSN: 0378-1119; 1879-0038
• DOI: 10.1016/j.gene.2008.09.029

Bacillus stearothermophilus infA encoding translation initiation factor IF1 was cloned and expressed in Escherichia coli and its transcript and protein product characterized. Although the functional properties of B. stearothermophilus and E. coli IF1, compared in several translational tests in the presence of both homologous and heterologous components, are not entirely identical, the two proteins are interchangeable in an in vitro translational system programmed with a natural mRNA. The availability of purified B. stearothermophilus IF1 now allows us to analyze the translation initiation pathway using efficient in vitro tests based entirely on purified components derived from this thermophilic Gram-positive bacterium.