Transfer of phosphoryl group between two regulatory proteins involved in osmoregulatory expression of the ompF and ompC genes in Escherichia coli.

نویسندگان

  • H Aiba
  • T Mizuno
  • S Mizushima
چکیده

EnvZ is a cytoplasmic membrane protein which is involved in osmoregulatory expression of the ompF and ompC genes in Escherichia coli possibly by sensing the environmental osmotic signal. A truncated form of the EnvZ protein (EnvZ*), comprising 82% of EnvZ starting from the C terminus, was purified to homogeneity. The purified EnvZ* was autophosphorylated with ATP. The phosphoryl group on EnvZ* could then be rapidly transferred to OmpR, which is a positive regulator of the ompF and ompC genes and which was proposed to interact with EnvZ in the process of osmoregulation. In the presence of ATP, the phosphorylated OmpR was rapidly dephosphorylated. These results suggest that the transfer of the phosphoryl group between EnvZ and OmpR plays an important role in the signaling pathway in osmoregulation.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Purification and characterization of the OmpR protein, a positive regulator involved in osmoregulatory expression of the ompF and ompC genes in Escherichia coli.

The OmpR protein is a positive regulator involved in osmoregulatory expression of the ompF and ompC genes, which respectively code for major outer membrane proteins OmpF and OmpC of Escherichia coli. The OmpR protein has been purified to homogeneity from an overproducing strain harboring an ompR gene-carrying plasmid. Throughout the purification the OmpR protein behaved as a single entity. The ...

متن کامل

Phosphorylation of OmpR by the osmosensor EnvZ modulates expression of the ompF and ompC genes in Escherichia coli.

EnvZ and OmpR, the regulatory proteins for ompF and ompC expression in Escherichia coli, belong to a modulator-effector family of regulatory proteins which are essential for the response to environmental signals. We show that the soluble cytoplasmic domain of the transmembrane modulator protein EnvZ is phosphorylated in vitro by [gamma-32P]-ATP. We also demonstrate that the phosphate group can,...

متن کامل

The leucine-responsive regulatory protein of Escherichia coli negatively regulates transcription of ompC and micF and positively regulates translation of ompF.

The two major porins of Escherichia coli K-12 strains, OmpC and OmpF, are inversely regulated with respect to one another. The expression of OmpC and OmpF has been shown to be influenced by the leucine-responsive regulatory protein (Lrp): two-dimensional gel electrophoresis of proteins from strains with and strains without a functional Lrp protein revealed that OmpC expression is increased in a...

متن کامل

Cloning and sequencing of ompf Salmonella typhi Salmonella ompf gene in Escherichia coli Origami

Background and Aim: Salmonella Typhi belongs to the family Enterobacteriaceae, gram-negative bacilli and causes gastrointestinal diseases such as typhoid. This bacterium has a special structure and various genes, including the ompf gene (outer membrane protein). Recent studies have shown the possibility of using ompf in the development of a diagnostic tuberculosis vaccine. Therefore, the aim of...

متن کامل

Heterologous expression of Escherichia coli porin genes in Salmonella typhi Ty2: regulation by medium osmolarity, temperature and oxygen availability.

Electrophoretic analysis of outer membrane proteins showed that Salmonella typhi OmpC expression is not reciprocally regulated relative to OmpF as described for Escherichia coli and S. typhimurium. When bacteria were grown in minimal media, both OmpC and OmpF were repressed as the osmolarity increased. However, in Luria broth, expression of OmpC was slightly induced by osmolarity up to 0.3 osmM...

متن کامل

ذخیره 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 نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 264 15  شماره 

صفحات  -

تاریخ انتشار 1989