99D-16 |
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L. TU, Food Science, University of Missouri - Columbia, 256 William Stringer Wing, Eckles Hall, University of Missouri, Columbia, MO 65211, F. Du, Genome Sequencing Center, Washington University School of Medicine, 4444 Forest Park Boulevard, St Louis, MO 63108, and A. Mustapha, Department of Food Science, University of Missouri, 256 Eckles Hall - Stringer Wing, Columbia, MO 65211. Ribosomal proteins are involved in the translational control of gene expression. Ribosomal protein engineering is receiving increasing attention as a tool to modify growth-related control mechanisms. Bifidobacteria are important microorganisms in foods, especially dairy products, and this has resulted in considerable efforts to understand their genes and gene regulations. However, no data on the ribosomal proteins or their genes in bifidobacteria are available. Knowledge of the structure of ribosomal proteins is essential to elucidate their role in the mechanism of ribosomal protein control in bifidobacteria. Our objectives were to clone and sequence the ribosomal protein gene from Bifidobacterium infantis . A genomic DNA library of B. infantis 15702 was constructed in l phage and 5 positive clones were further analyzed. Sequencing was performed by primer walking from both directions of the cloned DNA. One open reading frame spanning 1163 bp on the 3280-bp DNA fragment was located. It started with the ATG codon at position 280 and terminated with the TAA stop codon at position 1443. Comparative analysis of the nucleotide sequence with the sequence databases revealed that the highest identity, 59.9%, was found between the 50S ribosomal protein L9 of B. infantis 15702 and Rickettsia conorii Malish 7. The deduced amino acid sequence consists of 388 residues. The structure of bifidobacterial ribosomal protein gene will provide the basis for genetic approaches that will lead to a better understanding of this important organism and the mechanism of ribosomal protein control in bifidobacteria.
Session 99D, Food Microbiology: General
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