Abstract:
:The rotA gene of Escherichia coli encodes a peptidyl-prolyl cis/trans isomerase (PPIase), which is supposed to catalyse protein folding in the periplasm. To investigate the importance of the enzyme, the rotA gene was cloned and a chromosomal deletion mutant was created. The rotA mutant was normally viable. No residual PPIase activity could be detected in the periplasmic fraction of the mutant. Comparison of the patterns of periplasmic and outer membrane proteins by SDS-PAGE revealed no differences in protein composition between the rotA mutant and its parental strain. Similarly, the kinetics of periplasmic protein folding and outer membrane protein assembly appeared unaffected by the rotA mutation. Our results show that the periplasmic PPIase of E. coli is not essential and that the protein does not play an important role in protein folding.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Kleerebezem M,Heutink M,Tommassen Jdoi
10.1111/j.1365-2958.1995.mmi_18020313.xsubject
Has Abstractpub_date
1995-10-01 00:00:00pages
313-20issue
2eissn
0950-382Xissn
1365-2958journal_volume
18pub_type
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