Type III Protein Translocase HrcN IS A PERIPHERAL MEMBRANE ATPASE THAT IS ACTIVATED BY OLIGOMERIZATION*

نویسندگان

  • Charalambos Pozidis
  • Aggeliki Chalkiadaki
  • Amalia Gomez-Serrano
  • Henning Stahlberg
  • Ian Brown
  • Anastasia P. Tampakaki
  • Ariel Lustig
  • Giorgos Sianidis
  • Anastasia S. Politou
  • Andreas Engel
  • Nickolas J. Panopoulos
  • John Mansfield
  • Anthony P. Pugsley
  • Spyridoula Karamanou
  • Anastassios Economou
چکیده

From the Institute of Molecular Biology and Biotechnology, FORTH and Department of Biology, University of Crete, P.O. Box 1527, GR-711 10 Iraklio, Crete, Greece, §M.E. Mueller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland, the ¶Department of Biological Sciences, Imperial College at Wye, University of London, Ashford, Kent, United Kingdom TN25 5AH, the Laboratory of Biological Chemistry, Medical School, University of Ioaninna, Ioannina 45110 Greece, and the **Molecular Genetics Unit CNRS FRE 2364, Institut Pasteur, 25 Rue du Dr. Roux, 75724 Paris Cedex 15, France

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

Double hexameric ring assembly of the type III protein translocase ATPase HrcN.

The specialized type III secretion (T3S) apparatus of pathogenic and symbiotic Gram-negative bacteria comprises a complex transmembrane organelle and an ATPase homologous to the F1-ATPase beta subunit. The T3S ATPase HrcN of Pseudomonas syringae associates with the inner membrane, and its ATP hydrolytic activity is stimulated by dodecamerization. The structure of dodecameric HrcN (HrcN12) deter...

متن کامل

Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly.

FliI is the peripheral membrane ATPase pivotal to the type III protein export mechanism underlying the assembly of the bacterial flagellum. Gel filtration and multiangle light scattering showed that purified soluble native FliI protein was in a monomeric state but, in the presence of ATP, FliI showed a propensity to oligomerize. Electron microscopy revealed that FliI assembles to a ring structu...

متن کامل

Purification of a functional mature region from a SecA-dependent preprotein.

Most of the bacterial proteins that are active in extracytoplasmic locations are translocated through the inner membrane by the Sec translocase. Translocase comprises a membrane "pore" and the peripheral ATPase SecA. Where preproteins bind to SecA and how they activate translocation ATPase remains elusive. To address this central question we have purified to homogeneity the mature and preprotei...

متن کامل

O-10: A Marked Animal-Vegetal Polarity in The Localization of Na+,K+-ATPase Activity and Its Down-Regulation Following Progesterone-Induced Maturation

Background: Polarized cells are key to the process of differentiation. Xenopus oocyte is a polarized cell that has complete blue-print to differentiate 3 germ layers following fertilization, as key determinant molecules (Proteins and RNAs) are asymmetrically localized. The objective of this work was to localize Na+, K+-ATPase activity along animal-vegetal axis of polarized Xenopus oocyte and fo...

متن کامل

HrcQ Provides a Docking Site for Early and Late Type III Secretion Substrates from Xanthomonas

Pathogenicity of many Gram-negative bacteria depends on a type III secretion (T3S) system which translocates bacterial effector proteins into eukaryotic cells. The membrane-spanning secretion apparatus is associated with a cytoplasmic ATPase complex and a predicted cytoplasmic (C) ring structure which is proposed to provide a substrate docking platform for secreted proteins. In this study, we s...

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   شماره 

صفحات  -

تاریخ انتشار 2003