[Molecular mechanism of suppressing lambda N gene's expression in E. coli ribosomal protein S12 streptomycin-dependent mutant].
Using the polymerase chain reaction (PCR) method, the rpsLd gene was amplified and cloned, which encodes the streptomycin-dependent (Smd) mutant of ribosomal protein S12 in E.coli T83. The result of DNA sequencing showed an AAA to CAA mutation at codon 42, leading to the substitution of glutamine (Gln, Q) for lysine (Lys, K). According to the principle of Garnier, we predicted that there might be alterations in the secondary structural propensity of protein S12 due to the mutation. The outcome indicated that the beta-turn propensity at position 42 and its nearby region was increased evidently and the relative position of relevant subdomains were changed. As a result, the special conformation of the whole protein S12 was influenced. In view of that ribosomal proteins and ribosomal RNAs (rRNA) mutually adapted in structures and functions, the probable molecular mechanism. That how protein S12 Smd mutant in E.coli T83 suppressed lambda N gene's expression is discussed.
Jiang
X
X
Institute of Genetics, Academia Sinica, Beijing.
Weng
M
M
D000595:Amino Acid Sequence; D010582:Bacteriophage lambda / Q000235:genetics*; D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics*; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D012269:Ribosomal Proteins / Q000737:chemistry / Q000235:genetics*; D013307:Streptomycin / Q000494:pharmacology*
D012269:Ribosomal Proteins; C034212:ribosomal protein S12; D013307:Streptomycin