Skip to main content

Main menu

  • For Authors
    • Submit a Manuscript
    • Instructions for Authors
  • Home
  • Content
    • Current Issue
    • Archive
    • Preview Papers
    • Focus Collections
    • Classics Collection
    • Upcoming Focus Issues
  • Advertisers
  • About
    • About the Journal
    • Editorial Board and Staff
  • Subscribers
  • Librarians
  • More
    • Alerts
    • Contact Us
  • Other Publications
    • Plant Physiology
    • The Plant Cell
    • Plant Direct
    • The Arabidopsis Book
    • Plant Cell Teaching Tools
    • ASPB
    • Plantae

User menu

  • My alerts
  • Log in

Search

  • Advanced search
Plant Physiology
  • Other Publications
    • Plant Physiology
    • The Plant Cell
    • Plant Direct
    • The Arabidopsis Book
    • Plant Cell Teaching Tools
    • ASPB
    • Plantae
  • My alerts
  • Log in
Plant Physiology

Advanced Search

  • For Authors
    • Submit a Manuscript
    • Instructions for Authors
  • Home
  • Content
    • Current Issue
    • Archive
    • Preview Papers
    • Focus Collections
    • Classics Collection
    • Upcoming Focus Issues
  • Advertisers
  • About
    • About the Journal
    • Editorial Board and Staff
  • Subscribers
  • Librarians
  • More
    • Alerts
    • Contact Us
  • Follow plantphysiol on Twitter
  • Visit plantphysiol on Facebook
  • Visit Plantae
Research ArticleBIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES
Open Access

MAM3 Catalyzes the Formation of All Aliphatic Glucosinolate Chain Lengths in Arabidopsis

Susanne Textor, Jan-Willem de Kraker, Bettina Hause, Jonathan Gershenzon, James G. Tokuhisa
Susanne Textor
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Jan-Willem de Kraker
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Bettina Hause
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Jonathan Gershenzon
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
James G. Tokuhisa
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site

Published May 2007. DOI: https://doi.org/10.1104/pp.106.091579

  • Article
  • Figures & Data
  • Info & Metrics
  • PDF
Loading

Article Figures & Data

Figures

  • Tables
  • Additional Files
  • Figure 1.
    • Download figure
    • Open in new tab
    • Download powerpoint
    Figure 1.

    Scheme of Met-derived glucosinolate biosynthesis in Arabidopsis. This process can be divided into the Met chain elongation cycle (I) and the biosynthesis of the core glucosinolate structure (II). The parent methylthioalkyl glucosinolates can undergo further side chain modifications.

  • Figure 2.
    • Download figure
    • Open in new tab
    • Download powerpoint
    Figure 2.

    Immunocytochemical localization of MAM3 protein in Arabidopsis leaves. Cross section of leaves were probed with anti-MAM3 antibody (A and C) or with preimmune serum (E) followed by a fluorescence-labeled secondary antibody. A strong green fluorescence label within chloroplasts in A and C is indicative of the MAM3 protein. Chloroplasts are defined by positive 4,6-diamidino-2-phenylindole staining (B) of the same section as shown in A and by starch granules visualized in D by the differential interference contrast image of C. Negative control performed by treatment with preimmune serum did not exhibit any label (E). Bars = 20 μm in A, B, E, and 5 μm in C and D.

  • Figure 3.
    • Download figure
    • Open in new tab
    • Download powerpoint
    Figure 3.

    Glucosinolate profile of leaves (A) and seeds (B) of MAM3 mutants compared to Col-0 wild type. Glucosinolates were purified as desulfoglucosinolates, fractionated by reverse-phase HPLC, and individually identified and quantified. Individual Met-derived glucosinolates are grouped according to their chain length (no. of methylene carbons in the R group, C2–C8), while indole glucosinolates are depicted separately. Data show the means and ses of three replicate samples.

  • Figure 4.
    • Download figure
    • Open in new tab
    • Download powerpoint
    Figure 4.

    Glucosinolate profile of leaves (A) and seeds (B) of the MAM1 insertion mutant gsm1-3 compared to Col-0 wild type. Aliphatic glucosinolates sum up to 22.4/87.2 μmol g−1 dry weight (leaf/seed) in wild type and 27.3/96.9 μmol g−1 dry weight in the mutant. Glucosinolates were isolated, identified, and quantified as explained in the Figure 3 legend.

  • Figure 5.
    • Download figure
    • Open in new tab
    • Download powerpoint
    Figure 5.

    Steady-state mRNA transcript levels of MAM1 and MAM3 in tissues of Col-0 wild-type and MAM3 mutant lines determined by RT-PCR. DNA fragments for individual transcripts of ACT8 (actin), MAM1, and MAM3 were generated by PCR amplification of products from RT activity primed by oligo(dT) hybridization to the RNA. The PCR products are shown after separation on 1% agarose gels stained with ethidium bromide. Tissue source: 1, roots; 2, mature leaves; 3, expanding leaves; 4, flowers; and 5, siliques.

Tables

  • Figures
  • Additional Files
    • View popup
    Table I.

    Nomenclature for Arabidopsis (Col-0) genes of the IPMS/MAM synthase gene family used in recent publications

    Arabidopsis Genome Initiative Locus CodeN-Terminal SequenceBacterial Artificial ChromosomesKroymann et al. (2001)Junk and Mourad (2002)Field et al. (2004)This Article
    At1g18500MASSLLRF15H18–EST116C2T7MAML-4IPMS1
    At1g74040MESSILKF2P9.9–IMS1MAML-3IPMS2
    At5g23010MASSLLTCT20O7MAM1IMS3MAM1/LMAM1
    –aMASSLLTb––––MAM2
    At5g23020MASLLLTMYJ24MAM-LIMS2MAM1/LMAM3
    • ↵a Col-0 ecotype lacks MAM2. The gene would be located between At5g23000 and At5g23010 (MAM1) on the Col-0 genome (Kroymann et al., 2003).

    • ↵b Landsberg erecta.

    • View popup
    Table II.

    Suitability of 2-oxo acids as substrates for MAM3-mediated condensation with acetyl-CoA

    2-Oxo Acid SubstrateStructureResulting GlucosinolateSuitabilitya
    4-Methylthio-2-oxobutanoateEmbedded ImageC3+
    2-Oxo-hexanoateEmbedded ImageC3+
    5-Methylthio-2-oxopentanoateEmbedded ImageC4+
    2-Oxo-heptanoateEmbedded ImageC4+
    6-Methylthio-2-oxohexanoateEmbedded ImageC5+
    2-Oxo-octanoateEmbedded ImageC5+
    2-Oxo-nonanoateEmbedded ImageC6+
    8-Methylthio-2-oxooctanoateEmbedded ImageC7+
    2-Oxo-decanoateEmbedded ImageC7+
    9-Methylthio-2-oxononanoateEmbedded ImageC8+
    2-Oxo-undecanoateEmbedded ImageC8+
    2-Oxo-dodecanoateEmbedded ImageC9−
    • ↵a +, Condensation product formed; −, condensation product not formed.

    • View popup
    Table III.

    Kinetic parameters for various 2-oxo acids with recombinant MAM3a

    SubstrateKmVmaxkcatkcat/Km
    μmnmol min−1mg−1s−1m−1s−1
    4-Methylthio-2-oxobutanoic acid (→C3 glucosinolates)932 ± 561,448 ± 2991.3 ± 0.31,380
    5-Methylthio-2-oxopentanoic acid (→C4 glucosinolates)476 ± 1991,495 ± 6791.3 ± 0.62,730
    6-Methylthio-2-oxohexanoic acid (→C5 glucosinolates)463 ± 2102,869 ± 7682.5 ± 0.75,400
    8-Methylthio-2-oxooctanoic acid (→C7 glucosinolates)253 ± 123364 ± 1430.3 ± 0.11,280
    9-Methylthio-2-oxononanoic acid (→C8 glucosinolates)81 ± 2131 ± 80.03 ± 0.01370
    2-Oxoisovalerate1,000 ± 200199 ± 380.18 ± 0.03200
    Pyruvate8,600 ± 4,300191 ± 480.17 ± 0.0423
    Acetyl-CoA2,300 ± 1,2003,344 ± 14283.0 ± 1.31,300
    • ↵a Data presented are means ± sds of at least five replicates per substrate.

    • View popup
    Table IV.

    Glucosinolate content (μmol g−1 dry weight) in leaves of gsm2-1 and lines transformed with 35S∷MAM3a

    LineC3C4C5C6C7C8ΣCi
    Col-0 wild type2.716.30.50.30.42.222.4
    gsm2-12.518.20.60.2n.d.n.d.21.5
    T2 Line 12.36.5n.d.1.03.28.621.6
    T2 Line 23.98.0n.d.1.66.215.935.5
    T2 Line 34.16.4n.d.1.13.910.125.7
    • ↵a Presented are analyses of Col-0 wild type, the gsm2-1 parent line, and three lines randomly selected from a T2 segregating population that had detectable levels of the introduced MAM3 transcript. n.d., Not detected.

Additional Files

  • Figures
  • Tables
  • Supplemental Data

    Supplemental Figures and Table

    Files in this Data Supplement:

    • Supplemental Data - Supplemental Figures and Table
PreviousNext
Back to top

Table of Contents

Print
Download PDF
Email Article

Thank you for your interest in spreading the word on Plant Physiology.

NOTE: We only request your email address so that the person you are recommending the page to knows that you wanted them to see it, and that it is not junk mail. We do not capture any email address.

Enter multiple addresses on separate lines or separate them with commas.
MAM3 Catalyzes the Formation of All Aliphatic Glucosinolate Chain Lengths in Arabidopsis
(Your Name) has sent you a message from Plant Physiology
(Your Name) thought you would like to see the Plant Physiology web site.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Citation Tools
MAM3 Catalyzes the Formation of All Aliphatic Glucosinolate Chain Lengths in Arabidopsis
Susanne Textor, Jan-Willem de Kraker, Bettina Hause, Jonathan Gershenzon, James G. Tokuhisa
Plant Physiology May 2007, 144 (1) 60-71; DOI: 10.1104/pp.106.091579

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
Request Permissions
Share
MAM3 Catalyzes the Formation of All Aliphatic Glucosinolate Chain Lengths in Arabidopsis
Susanne Textor, Jan-Willem de Kraker, Bettina Hause, Jonathan Gershenzon, James G. Tokuhisa
Plant Physiology May 2007, 144 (1) 60-71; DOI: 10.1104/pp.106.091579
del.icio.us logo Digg logo Reddit logo Twitter logo CiteULike logo Facebook logo Google logo Mendeley logo
  • Tweet Widget
  • Facebook Like
  • Google Plus One

Jump to section

  • Article
    • Abstract
    • RESULTS
    • DISCUSSION
    • MATERIALS AND METHODS
    • Acknowledgments
    • Footnotes
    • LITERATURE CITED
  • Figures & Data
  • Info & Metrics
  • PDF

In this issue

Plant Physiology: 144 (1)
Plant Physiology
Vol. 144, Issue 1
May 2007
  • Table of Contents
  • Table of Contents (PDF)
  • About the Cover
  • Index by author
  • Advertising (PDF)
  • Back Matter (PDF)
  • Ed Board (PDF)
  • Front Matter (PDF)
View this article with LENS

More in this TOC Section

  • Decreasing the Mitochondrial Synthesis of Malate in Potato Tubers Does Not Affect Plastidial Starch Synthesis, Suggesting That the Physiological Regulation of ADPglucose Pyrophosphorylase Is Context Dependent
  • UDP-Glycosyltransferases from the UGT73C Subfamily in Barbarea vulgaris Catalyze Sapogenin 3-O-Glucosylation in Saponin-Mediated Insect Resistance
  • Tie-dyed2 Encodes a Callose Synthase That Functions in Vein Development and Affects Symplastic Trafficking within the Phloem of Maize Leaves
Show more BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES

Similar Articles

Our Content

  • Home
  • Current Issue
  • Plant Physiology Preview
  • Archive
  • Focus Collections
  • Classic Collections
  • The Plant Cell
  • Plant Direct
  • Plantae
  • ASPB

For Authors

  • Instructions
  • Submit a Manuscript
  • Editorial Board and Staff
  • Policies
  • Recognizing our Authors

For Reviewers

  • Instructions
  • Journal Miles
  • Policies

Other Services

  • Permissions
  • Librarian resources
  • Advertise in our journals
  • Alerts
  • RSS Feeds

Copyright © 2021 by The American Society of Plant Biologists

Powered by HighWire