Advertisement
JBC

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


     


Originally published In Press as doi:10.1074/jbc.M601183200 on April 24, 2006

J. Biol. Chem., Vol. 281, Issue 26, 17900-17908, June 30, 2006
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
281/26/17900    most recent
M601183200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
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 arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pikis, A.
Right arrow Articles by Thompson, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pikis, A.
Right arrow Articles by Thompson, J.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Genetic Requirements for Growth of Escherichia coli K12 on Methyl-{alpha}-D-glucopyranoside and the Five {alpha}-D-Glucosyl-D-fructose Isomers of Sucrose*

Andreas Pikis{ddagger}1, Sonja Hess§, Ingrid Arnold, Bernhard Erni, and John Thompson{ddagger}2

From the {ddagger}Microbial Biochemistry and Genetics Unit, Oral Infection and Immunity Branch, NIDCR, and the §Proteomics and Mass Spectrometry Facility, NIDDK, National Institutes of Health, Department of Health and Human Services, Bethesda, Maryland 20892 and the Departement für Chemie und Biochemie, Universität Bern, CH-3012 Bern, Switzerland

Strains of Escherichia coli K12, including MG-1655, accumulate methyl-{alpha}-D-glucopyranoside via the phosphoenolpyruvate-dependent glucose:phosphotransferase system (IICBGlc/IIAGlc). High concentrations of intracellular methyl-{alpha}-D-glucopyranoside 6-phosphate are toxic, and cell growth is prevented. However, transformation of E. coli MG-1655 with a plasmid (pAP1) encoding the gene aglB from Klebsiella pneumoniae resulted in excellent growth of the transformant MG-1655 (pAP1) on the glucose analog. AglB is an unusual NAD+/Mn2+-dependent phospho-{alpha}-glucosidase that promotes growth of MG-1655 (pAP1) by catalyzing the in vivo hydrolysis of methyl-{alpha}-D-glucopyranoside 6-phosphate to yield glucose 6-phosphate and methanol. When transformed with plasmid pAP2 encoding the K. pneumoniae genes aglB and aglA (an {alpha}-glucoside-specific transporter AglA (IICBAgl)), strain MG-1655 (pAP2) metabolized a variety of other {alpha}-linked glucosides, including maltitol, isomaltose, and the following five isomers of sucrose: trehalulose {alpha}(1->1), turanose {alpha}(1->3), maltulose {alpha}(1->4), leucrose {alpha}(1->5), and palatinose {alpha}(1->6). Remarkably, MG-1655 (pAP2) failed to metabolize sucrose {alpha}(1->2). The E. coli K12 strain ZSC112L (ptsG::cat manXYZ nagE glk lac) can neither grow on glucose nor transport methyl-{alpha}-D-glucopyranoside. However, when transformed with pTSGH11 (encoding ptsG) or pAP2, this organism provided membranes that contained either the PtsG or AglA transporters, respectively. In vitro complementation of transporter-specific membranes with purified general phosphotransferase components showed that although PtsG and AglA recognized glucose and methyl-{alpha}-D-glucopyranoside, only AglA accepted other {alpha}-D-glucosides as substrates. Complementation experiments also revealed that IIAGlc was required for functional activity of both PtsG and AglA transporters. We conclude that AglA, AglB, and IIAGlc are necessary and sufficient for growth of E. coli K12 on methyl-{alpha}-D-glucoside and related {alpha}-D-glucopyranosides.


Received for publication, February 7, 2006 , and in revised form, March 27, 2006.

* This work was supported by the NIDCR and NIDDK Intramural Research Programs, National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

1 Present address: Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20993.

2 To whom correspondence should be addressed: NIDCR, National Institutes of Health, Bldg. 30, Rm. 325, Convent Dr. MSC-4350, Bethesda, MD 20892. Tel.: 301-496-4083; Fax: 301-402-1064; E-mail: jthompson{at}dir.nidcr.nih.gov.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Bacteriol.Home page
J. Thompson, N. Jakubovics, B. Abraham, S. Hess, and A. Pikis
The sim Operon Facilitates the Transport and Metabolism of Sucrose Isomers in Lactobacillus casei ATCC 334
J. Bacteriol., May 1, 2008; 190(9): 3362 - 3373.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2006 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement