ISSN:
0091-7419
Keywords:
Life Sciences
;
Molecular Cell Biology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
The assembly of E. coli ribosomes has been studied through the analysis of a new group of ribosome maturation mutants. These mutants, all blocked in a late stage in the maturation of 50S ribosomes, map at four different sites on the chromosome. These sites are distant from the known ribosomal protein sites at the str-aro E region of the chromosome. The ribosome precursor particles of the mutants contain precursor-type 23S RNA (p23 RNA) and 5S RNA. 43S particles of one of the mutants contain all but one of the normal complement of proteins. Precursor 43S particles from this mutant can be converted to particles with sedimentation values around 50S by incubation with extracts from either the wild-type organism or from other mutants. This in vitro conversion process differs considerably from the process of ribosome reconstitution and indicates a role for extrinsic factors in the maturation of E. coli ribosomes.
Additional Material:
8 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/jss.400020211
