English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  The magnetosome proteins MamX, MamZ and MamH are involved in redox control of magnetite biomineralization in Magnetospirillum gryphiswaldense

Raschdorf, O., Mueller, F. D., Posfai, M., Plitzko, J. M., & Schueler, D. (2013). The magnetosome proteins MamX, MamZ and MamH are involved in redox control of magnetite biomineralization in Magnetospirillum gryphiswaldense. MOLECULAR MICROBIOLOGY, 89(5), 872-886. doi:10.1111/mmi.12317.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Raschdorf, Oliver1, Author           
Mueller, Frank D.2, Author
Posfai, Mihaly2, Author
Plitzko, Jürgen M.1, Author           
Schueler, Dirk2, Author
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              

Content

show
hide
Free keywords: MAJOR FACILITATOR SUPERFAMILY; C-TYPE CYTOCHROME; MAGNETOTACTIC BACTERIA; PROTEOMIC ANALYSIS; MEMBRANE; REVEALS; ISLAND; DELETION; GROWTH; ACTIN
 Abstract: Magnetospirillum gryphiswaldense uses intracellular chains of membrane-enveloped magnetite crystals, the magnetosomes, to navigate within magnetic fields. The biomineralization of magnetite nanocrystals requires several magnetosome-associated proteins, whose precise functions so far have remained mostly unknown. Here, we analysed the functions of MamX and the Major Facilitator Superfamily (MFS) proteins MamZ and MamH. Deletion of either the entire mamX gene or elimination of its putative haem c-binding magnetochrome domains, and deletion of either mamZ or its C-terminal ferric reductase-like component resulted in an identical phenotype. All mutants displayed WT-like magnetite crystals, flanked within the magnetosome chains by poorly crystalline flake-like particles partly consisting of haematite. Double deletions of both mamZ and its homologue mamH further impaired magnetite crystallization in an additive manner, indicating that the two MFS proteins have partially redundant functions. Deprivation of mamX and mamZ cells from nitrate, or additional loss of the respiratory nitrate reductase Nap from mamX severely exacerbated the magnetosome defects and entirely inhibited the formation of regular crystals, suggesting that MamXZ and Nap have similar, but independent roles in redox control of biomineralization. We propose a model in which MamX, MamZ and MamH functionally interact to balance the redox state of iron within the magnetosome compartment.

Details

show
hide
Language(s): eng - English
 Dates: 2013-09
 Publication Status: Issued
 Pages: 15
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000323647700006
DOI: 10.1111/mmi.12317
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: MOLECULAR MICROBIOLOGY
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: 111 RIVER ST, HOBOKEN 07030-5774, NJ USA : WILEY-BLACKWELL
Pages: - Volume / Issue: 89 (5) Sequence Number: - Start / End Page: 872 - 886 Identifier: ISSN: 0950-382X