Changes in ribosomal proteins associated with mutants in a locus that affects Escherichia coli ribosomes |
| |
| Authors: | J Krembel D Apirion |
| |
| Affiliation: | 1. Novartis Institutes for Biomedical Research, Novartis Campus, CH-4056 Basel, Switzerland;2. University of Salzburg, Department of Biosciences and Medical Biology, Hellbrunnerstrasse 34, 5020 Salzburg, Austria;3. GMP Unit, Spinal Cord Injury & Tissue Regeneration Center Salzburg (SCI-TReCS), Paracelsus Medical University, Salzburg, Austria;4. EvoBiotiX SA, Via Lungo Lago 86, 6815 Melide, Switzerland;1. State Key Joint Laboratory of Environmental Simulation and Pollution Control, College of Environmental Sciences and Engineering, Peking University, Beijing 100871, P.R. China;2. School of Environment, Tsinghua University, Beijing 100084; P.R. China |
| |
| Abstract: | The ribosomal proteins from four strains of Escherichia coli, containing mutations in a locus that affect 50 s ribosomes (the lir locus), were compared to the parental wild-type strain by electrophoresis in polyacrylamide gels at pH 4.5. Two differences were found. (1) One band in the electrophoretic pattern obtained with 50 s ribosomal proteins prepared from the mutant strains migrated faster than the corresponding band in patterns obtained with wild-type 50 s ribosomal proteins. This band may possibly be the protein coded by the lir gene. (2) Two slow-moving bands absent in electrophoretic patterns of wild-type 50 s ribosomal proteins were observed in electropherograms of the 50 s ribosomal proteins of all four mutant strains. These bands contain relatively acidic proteins which may be related to normal 50s ribosomal proteins. We suggest that these proteins are weakly associated with ribosomal components in wild-type E. coli but become more strongly associated with them as a result of the lir mutation, and are therefore found in the 50 s ribosomal proteins isolated from lir mutants. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
