Dissociation of 70S ribosomes: some properties of the dissociating factor from Bacillus stearothermophilus and Escherichia coli.
نویسندگان
چکیده
A protein factor which produces in vitro dissociation of 70S particles into 30S and 50S subunits has been obtained from Bacillus stearothermophilus and Escherichia coli. The factor could be extracted from ribosomes, polyribosomes, and S100 supernatant. The kinetics and temperature curve of the dissociation process in the B. stearothermophilus system have been studied and compared with the reaction in the E. coli system. No species specificity was observed when hybrid mixtures of ribosomes and dissociating factor from both bacteria were used. The wide variations of dissociating activity in cells at different stages of growth and the capacity of the liberated subunits to carry out polypeptide synthesis suggest that the dissociating factor has a physiological role.
منابع مشابه
Isolation and properties of polypeptide chain initiation factor FII from Escherichia coli: evidence for a dual function.
Initiation factor FII (F(3), factor B) has been purified from Escherichia coli Q13 to apparent homogeneity. It is a heat-stable basic protein, consisting of a single polypeptide chain of molecular weight 21,000. FII is required, in addition to the other factors FI and FIII, for the formation of a 70S complex containing fMet-tRNA, poly(U,G) (used as a model messenger RNA), and the ribosome. FII ...
متن کاملIdentification of chloramphenicol-binding protein in Escherichia coli ribosomes by affinity labeling.
Monoiodoamphenicol, a synthetic analogue of chloramphenicol, has been shown by competition experiments with chloramphenicol and lincomycin to bind at the same site of 70S ribosomes as chloramphenicol. At - 2 degrees it forms a 1:1 complex with 70S ribosomes having a value of K (7.5 x 10(4) M(-1)) that is one order of magnitude lower than that of chloramphenicol. At 37 degrees , monoiodoamphenic...
متن کاملTranslation activity of chimeric ribosomes composed of Escherichia coli and Bacillus subtilis or Geobacillus stearothermophilus subunits
Ribosome composition, consisting of rRNA and ribosomal proteins, is highly conserved among a broad range of organisms. However, biochemical studies focusing on ribosomal subunit exchangeability between organisms remain limited. In this study, we show that chimeric ribosomes, composed of Escherichia coli and Bacillus subtilis or E. coli and Geobacillus stearothermophilus subunits, are active for...
متن کاملHeat stabilities of ribosomal subunits and reassociated ribosomes from Bacillus stearothermophilus.
Absorbance-temperature profiles reveal that both the 30S and 50S ribosomal subunits from Bacillus stearothermophilus are more thermostable than the comparable Escherichia coli particles. Thermophile ribosomes formed by the reassociation of subunits do not display functional heat stability.
متن کاملFunctional correspondence between 30S ribosomal proteins of Escherichia coli and Bacillus stearothermophilus.
30S ribosomal proteins from Bacillus stearothermophilus (B. proteins) have been fractionated and characterized with respect to their ability to replace various E. coli 30S proteins (E. proteins) in the E. coli 30S ribosome reconstitution system. The functional counterparts of all the E. proteins, except S1, S6, S9, and S13, have been tested. In all cases, B. proteins can substitute for E. prote...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 64 2 شماره
صفحات -
تاریخ انتشار 1969