The Escherichia coli Cell Division Protein and Model Tat Substrate SufI (FtsP) Localizes to the Septal Ring and Has a Multicopper Oxidase-Like Structure

نویسندگان

  • Michael Tarry
  • S.J. Ryan Arends
  • Pietro Roversi
  • Evan Piette
  • Frank Sargent
  • Ben C. Berks
  • David S. Weiss
  • Susan M. Lea
چکیده

The Escherichia coli protein SufI (FtsP) has recently been proposed to be a component of the cell division apparatus. The SufI protein is also in widespread experimental use as a model substrate in studies of the Tat (twin arginine translocation) protein transport system. We have used SufI-GFP (green fluorescent protein) fusions to show that SufI localizes to the septal ring in the dividing cell. We have also determined the structure of SufI by X-ray crystallography to a resolution of 1.9 A. SufI is structurally related to the multicopper oxidase superfamily but lacks metal cofactors. The structure of SufI suggests it serves a scaffolding rather than an enzymatic role in the septal ring and reveals regions of the protein likely to be involved in the protein-protein interactions required to assemble SufI at the septal ring.

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

Role of SufI (FtsP) in cell division of Escherichia coli: evidence for its involvement in stabilizing the assembly of the divisome.

The function of SufI, a well-studied substrate of the TatABC translocase in Escherichia coli, is not known. It was earlier implicated in cell division, based on the finding that multiple copies of sufI suppressed the phenotypes of cells with mutations in ftsI (ftsI23), which encodes a divisomal transpeptidase. Recently, sufI was identified as both a multicopy suppressor gene and a synthetic let...

متن کامل

Designing and analyzing the structure of Tat-BoNT/A(1-448) fusion protein: An in silico approach

Clostridium botulinum type A (BoNT/A) produces a neurotoxin recently found to be useful as an injectable drug for the treatment of abnormal muscle contractions. The catalytic domain of this toxin which is responsible for the main toxin activity is a zinc metalloprotease that inhibits the release of neurotransmitter mediators in neuromuscular junctions. A cell penetrating cationic peptide, Tat, ...

متن کامل

Functional reconstitution of bacterial Tat translocation in vitro.

The Tat (twin-arginine translocation) pathway is a Sec-independent mechanism for translocating folded preproteins across or into the inner membrane of Escherichia coli. To study Tat translocation, we sought an in vitro translocation assay using purified inner membrane vesicles and in vitro synthesized substrate protein. While membrane vesicles derived from wild-type cells translocate the Sec-de...

متن کامل

ATP-binding site lesions in FtsE impair cell division.

FtsE and FtsX of Escherichia coli constitute an apparent ABC transporter that localizes to the septal ring. In the absence of FtsEX, cells divide poorly and several membrane proteins essential for cell division are largely absent from the septal ring, including FtsK, FtsQ, FtsI, and FtsN. These observations, together with the fact that ftsE and ftsX are cotranscribed with ftsY, which helps to t...

متن کامل

Design and Production of Recombinant TAT Protein Structure, Catalytic Domain of Diphtheria Toxin, and Evaluation of Its Effect on Cell Line

Background and Objectives: Cancer is one of the most deadly diseases in the present age and its conventional therapies have had low success. Toxin therapy of cancer is a new therapeutic approach, which has attracted the attention of pharmaceutical specialists. Diphtheria toxin consists of three functional, transducing, and binding domains, that the functional part inhibits protein synthesis and...

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:

دوره 386  شماره 

صفحات  -

تاریخ انتشار 2009