Search anything and hit enter
  • Teams
  • Members
  • Projects
  • Events
  • Calls
  • Jobs
  • publications
  • Software
  • Tools
  • Network
  • Equipment

A little guide for advanced search:

  • Tip 1. You can use quotes "" to search for an exact expression.
    Example: "cell division"
  • Tip 2. You can use + symbol to restrict results containing all words.
    Example: +cell +stem
  • Tip 3. You can use + and - symbols to force inclusion or exclusion of specific words.
    Example: +cell -stem
e.g. searching for members in projects tagged cancer
Search for
Count
IN
OUT
Content 1
  • member
  • team
  • department
  • center
  • program_project
  • nrc
  • whocc
  • project
  • software
  • tool
  • patent
  • Administrative Staff
  • Assistant Professor
  • Associate Professor
  • Clinical Research Assistant
  • Clinical Research Nurse
  • Clinician Researcher
  • Department Manager
  • Dual-education Student
  • Full Professor
  • Honorary Professor
  • Lab assistant
  • Master Student
  • Non-permanent Researcher
  • Nursing Staff
  • Permanent Researcher
  • Pharmacist
  • PhD Student
  • Physician
  • Post-doc
  • Prize
  • Project Manager
  • Research Associate
  • Research Engineer
  • Retired scientist
  • Technician
  • Undergraduate Student
  • Veterinary
  • Visiting Scientist
  • Deputy Director of Center
  • Deputy Director of Department
  • Deputy Director of National Reference Center
  • Deputy Head of Facility
  • Director of Center
  • Director of Department
  • Director of Institute
  • Director of National Reference Center
  • Group Leader
  • Head of Facility
  • Head of Operations
  • Head of Structure
  • Honorary President of the Departement
  • Labex Coordinator
Content 2
  • member
  • team
  • department
  • center
  • program_project
  • nrc
  • whocc
  • project
  • software
  • tool
  • patent
  • Administrative Staff
  • Assistant Professor
  • Associate Professor
  • Clinical Research Assistant
  • Clinical Research Nurse
  • Clinician Researcher
  • Department Manager
  • Dual-education Student
  • Full Professor
  • Honorary Professor
  • Lab assistant
  • Master Student
  • Non-permanent Researcher
  • Nursing Staff
  • Permanent Researcher
  • Pharmacist
  • PhD Student
  • Physician
  • Post-doc
  • Prize
  • Project Manager
  • Research Associate
  • Research Engineer
  • Retired scientist
  • Technician
  • Undergraduate Student
  • Veterinary
  • Visiting Scientist
  • Deputy Director of Center
  • Deputy Director of Department
  • Deputy Director of National Reference Center
  • Deputy Head of Facility
  • Director of Center
  • Director of Department
  • Director of Institute
  • Director of National Reference Center
  • Group Leader
  • Head of Facility
  • Head of Operations
  • Head of Structure
  • Honorary President of the Departement
  • Labex Coordinator
Search

← Go to Research

Go back
Scroll to top
Share
© Research
Publication : Journal of Biological Chemistry

A carboxyl-terminal four-amino acid motif is required for secretion of the metalloprotease PrtG through the Erwinia chrysanthemi protease secretion pathway.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of Biological Chemistry - 25 Mar 1994

Ghigo J.-M., Wandersman C.

Link to Pubmed [PMID] – 8132636

J Biol Chem. 1994 Mar 25;269(12):8979-85.

PrtG is an extracellular metalloprotease secreted by the Gram-negative bacterium Erwinia chrysanthemi through a signal peptide-independent secretion pathway. Previous studies showed that the PrtG secretion signal is COOH-terminal and located in the last 56 residues of PrtG. We have now performed a deletion and elongation mapping of a short secretion competent COOH-terminal peptide CterG. This approach allowed us to show that: (i) the smaller COOH-terminal sequence containing the information necessary to promote the secretion of a small polypeptide is contained in the last 29 residues of PrtG; (ii) a low but significant level of secretion can be promoted by the last 15 residues of PrtG when fused to the COOH terminus of a non-secreted PrtG derivative; (iii) the extreme COOH-terminal sequence Dxxx, where xs are hydrophobic residues, is a conserved motif in all constructs that are secreted through the E. chrysanthemi transporter. (vi) This motif has to be COOH terminally exposed since addition of even one amino acid impairs the secretion of CterG. The extent of the secretion defect observed with the COOH terminally extended variants correlates with the length of the extension. These results indicate a key role for the COOH-terminal exposition of the last four amino acids in the secretion of PrtG.