Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Microbiology 149 (2003), 3437-3447; DOI  10.1099/mic.0.26518-0
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chandu, D.
Right arrow Articles by Nandi, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chandu, D.
Right arrow Articles by Nandi, D.
Agricola
Right arrow Articles by Chandu, D.
Right arrow Articles by Nandi, D.
Microbiology 149 (2003), 3437-3447; DOI  10.1099/mic.0.26518-0
© 2003 Society for General Microbiology

PepN is the major aminopeptidase in Escherichia coli: insights on substrate specificity and role during sodium-salicylate-induced stress

Dilip Chandu and Dipankar Nandi

Department of Biochemistry, Indian Institute of Science, Bangalore 560012, India

Correspondence
Dipankar Nandi
nandi{at}biochem.iisc.ernet.in

PepN and its homologues are involved in the ATP-independent steps (downstream processing) during cytosolic protein degradation. To obtain insights into the contribution of PepN to the peptidase activity in Escherichia coli, the hydrolysis of a selection of endopeptidase and exopeptidase substrates was studied in extracts of wild-type strains and two pepN mutants, 9218 and DH5{alpha}{Delta}pepN. Hydrolysis of three of the seven endopeptidase substrates tested was reduced in both pepN mutants. Similar studies revealed that hydrolysis of 10 of 14 exopeptidase substrates studied was greatly reduced in both pepN mutants. This decreased ability to cleave these substrates is pepN-specific as there is no reduction in the ability to hydrolyse exopeptidase substrates in E. coli mutants lacking other peptidases, pepA, pepB or pepE. PepN overexpression complemented the hydrolysis of the affected exopeptidase substrates. These results suggest that PepN is responsible for the majority of aminopeptidase activity in E. coli. Further in vitro studies with purified PepN revealed a preference to cleave basic and small amino acids as aminopeptidase substrates. Kinetic characterization revealed the aminopeptidase cleavage preference of E. coli PepN to be Arg>Ala>Lys>Gly. Finally, it was shown that PepN is a negative regulator of the sodium-salicylate-induced stress in E. coli, demonstrating a physiological role for this aminoendopeptidase under some stress conditions.

Abbreviations: AMC, 7-amino-4-methylcoumarin; {beta}NA, {beta}-naphthylamide; Boc, butoxycarbonyl; Cbz, benzoyloxycarbonyl; NaSal, sodium salicylate; pNA, p-nitroanilide




This article has been cited by other articles:


Home page
 Protein Eng Des SelHome page
J. Arima, Y. Uesugi, M. Iwabuchi, and T. Hatanaka
Streptomyces aminopeptidase P: biochemical characterization and insight into the roles of its N-terminal domain
Protein Eng. Des. Sel., January 1, 2008; 21(1): 45 - 53.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
P. C. Fineran, N. R. Williamson, K. S. Lilley, and G. P. C. Salmond
Virulence and Prodigiosin Antibiotic Biosynthesis in Serratia Are Regulated Pleiotropically by the GGDEF/EAL Domain Protein, PigX
J. Bacteriol., November 1, 2007; 189(21): 7653 - 7662.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
K. Tabata and S.-i. Hashimoto
Fermentative Production of L-Alanyl-L-Glutamine by a Metabolically Engineered Escherichia coli Strain Expressing L-Amino Acid {alpha}-Ligase
Appl. Envir. Microbiol., October 15, 2007; 73(20): 6378 - 6385.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Ito, Y. Nakajima, Y. Onohara, M. Takeo, K. Nakashima, F. Matsubara, T. Ito, and T. Yoshimoto
Crystal Structure of Aminopeptidase N (Proteobacteria Alanyl Aminopeptidase) from Escherichia coli and Conformational Change of Methionine 260 Involved in Substrate Recognition
J. Biol. Chem., November 3, 2006; 281(44): 33664 - 33676.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. Addlagatta, L. Gay, and B. W. Matthews
Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site
PNAS, September 5, 2006; 103(36): 13339 - 13344.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. Chavez-Gutierrez, E. Matta-Camacho, J. Osuna, E. Horjales, P. Joseph-Bravo, B. Maigret, and J.-L. Charli
Homology Modeling and Site-directed Mutagenesis of Pyroglutamyl Peptidase II: INSIGHTS INTO OMEGA-VERSUS AMINOPEPTIDASE SPECIFICITY IN THE M1 FAMILY
J. Biol. Chem., July 7, 2006; 281(27): 18581 - 18590.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
Y. Zheng, R. J. Roberts, S. Kasif, and C. Guan
Characterization of Two New Aminopeptidases in Escherichia coli
J. Bacteriol., June 1, 2005; 187(11): 3671 - 3677.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Malki, T. Caldas, J. Abdallah, R. Kern, V. Eckey, S. J. Kim, S.-S. Cha, H. Mori, and G. Richarme
Peptidase Activity of the Escherichia coli Hsp31 Chaperone
J. Biol. Chem., April 15, 2005; 280(15): 14420 - 14426.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2003 Society for General Microbiology.