PMID:2211695
| Citation |
Romero, DP, Arredondo, JA and Traut, RR (1990) Identification of a region of Escherichia coli ribosomal protein L2 required for the assembly of L16 into the 50 S ribosomal subunit. J. Biol. Chem. 265:18185-91 |
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| Abstract |
In vitro mutagenesis of rplB was used to generate changes in a conserved region of Escherichia coli ribosomal protein L2 between Gly221 and His231. Mutants were selected by temperature sensitivity using an inducible expression system. A mutant L2 protein with the deletion of Thr222 to Asp228 was readily distinguishable from wild-type L2 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and ribosomes from the strain overexpressing this mutant protein were characterized by sucrose density gradient centrifugation and protein composition. In addition to 30 S and 50 S ribosomal subunits, cell lysates contained a new component that sedimented at 40 S in 1 mM Mg2+ and at 48 S in 10 mM Mg2+. These particles contained mutant L2 protein exclusively, completely lacked L16, and had reduced amounts of L28, L33, and L34. They did not reassociate with 30 S ribosomal subunits and were inactive in polyphenylalanine synthesis. Other mutants in the same conserved region, including the substitution of His229 by Gln229, produced similar aberrant 50 S particles that sedimented at 40 S and failed to associate with 30 S subunits. |
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| Keywords |
Amino Acid Sequence; Centrifugation, Density Gradient; Cloning, Molecular; DNA Mutational Analysis; Electrophoresis, Gel, Two-Dimensional; Escherichia coli; Molecular Sequence Data; Morphogenesis; Protein Biosynthesis; Ribosomal Proteins/genetics; Ribosomal Proteins/metabolism; Ribosomes/physiology; Ribosomes/ultrastructure |
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