Characterization of a mutant form of ribosomal protein S1 from Escherichia coli.
An altered form of ribosomal protein S1 from a mutant of Escherichia coli has been isolated and characterized. The mutant protein (denoted m1-S1) has a molecular weight of 57,000 as shown by sodium dodecyl sulfate-gel electrophoresis and the same NH2-terminal sequence as wild type S1. Protein m1-S1 binds poly(U) in the same manner as protein S1 and is active in protein synthesis with either synthetic or natural mRNA. Thus, about 75% of the sequence of protein S1 (which includes the NH2-terminal region) contains essentially all the functional domains of this protein involved in protein biosynthesis.
D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000032:analysis* / Q000378:metabolism; D005779:Immunodiffusion; D007700:Kinetics; D009154:Mutation; D011072:Poly U; D014176:Protein Biosynthesis; D012269:Ribosomal Proteins / Q000032:analysis* / Q000378:metabolism
D012269:Ribosomal Proteins; D011072:Poly U