Deductive analysis of a protein-synthesis mutant of Escherichia coli |
| |
| Authors: | David Patterson David Gillespie |
| |
| Affiliation: | (1) Biology Department, Brandeis University, Waltham, Massachusetts, and Laboratory of Molecular Aging, Gerontology Research Center, NICHD, NIH, and the Baltimore City Hospitals, Baltimore, Maryland;(2) Present address: Department of Biophysics, University of Colorado Medical Center, Denver, Colorado;(3) Present address: Gerontology Research Center, Baltimore City Hospitals, Baltimore, Maryland |
| |
| Abstract: | A mutant of E. coli, Ts68b, selected as unable to grow at 43 C, is unable to synthesize proteins at 43 C, though it can carry out this function at 30 C. This defect is shown to be in the protein-synthetic rather than the RNA-synthetic machinery by an analysis of the response of the strain to infection with the RNA bacteriophage f2. An analysis of the capacity for RNA synthesis and the polyribosome content of these cells at 44 C indicates that the defect resides in the elongation step of protein synthesis. No defects could be detected in vitro. The results are discussed in light of similar data on other mutants and in relation to the general approach of analyzing complex mutants selected with ill-defined phenotypes.This work was supported by Grant GM14368 from the National Institute of Health. |
| |
| Keywords: | |
| 本文献已被 SpringerLink 等数据库收录！ |
|
