Subunit association defects in Escherichia coli ribosome mutants lacking proteins S20 and L11
نویسندگان
چکیده
منابع مشابه
Mutant DnaK chaperones cause ribosome assembly defects in Escherichia coli.
To determine whether the biogenesis of ribosomes in Escherichia coli is the result of the self-assembly of their different constituents or involves the participation of additional factors, we have studied the influence of a chaperone, the product of the gene dnaK, on ribosome assembly in vivo. Using three thermosensitive (ts) mutants carrying the mutations dnaK756-ts, dnaK25-ts, and dnaK103-ts,...
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Membrane-derived oligosaccharides (MDO) consist of branched substituted beta-glucan chains and are present in the periplasmic space of Escherichia coli and other gram-negative bacteria. A procedure for the isolation of mutants defective in MDO synthesis is described. Their phenotype was compared with a mdoA mutant previously identified, and they are mapped in the mdoA region. Mutants lacking MD...
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Previously, we constructed a set of mutants from which eight penicillin binding protein (PBP) genes were deleted in 192 combinations from Escherichia coli (S. A. Denome, P. K. Elf, T. A. Henderson, D. E. Nelson, and K. D. Young, J. Bacteriol. 181:3981-3993, 1999). Although these mutants were constructed correctly as determined by restriction mapping and the absence of relevant protein products,...
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The penicillin binding proteins (PBPs) synthesize and remodel peptidoglycan, the structural component of the bacterial cell wall. Much is known about the biochemistry of these proteins, but little is known about their biological roles. To better understand the contributions these proteins make to the physiology of Escherichia coli, we constructed 192 mutants from which eight PBP genes were dele...
متن کاملThe crystallization of ribosomal proteins from the 50 S subunit of the Escherichia coli and Bacillus stearothermophilus ribosome.
Several individual intact ribosomal proteins purified from bacterial sources under mild conditions have been crystallized. A number of these are suitable candidates for three-dimensional structural studies by x-ray diffraction techniques. Data collection to 3 A resolution for one of these proteins is in progress.
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1989
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1989.tb14890.x