Dataset Information

Crystallization and preliminary crystallographic analysis of the Magnetospirillum magneticum AMB-1 and M. gryphiswaldense MSR-1 magnetosome-associated proteins MamA.

ABSTRACT: MamA is a unique magnetosome-associated protein that is predicted to contain six sequential tetratricopeptide-repeat (TPR) motifs. The TPR structural motif serves as a template for protein-protein interactions and mediates the assembly of multi-protein complexes. Here, the crystallization and preliminary X-ray analysis of recombinant and purified Magnetospirillum magneticum and M. gryphiswaldense MamA are reported for the first time. M. gryphiswaldense MamADelta41 crystallized in the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 58.88, c = 144.09 A. M. magneticum MamADelta41 crystallized in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 44.75, b = 76.19, c = 105.05 A. X-ray diffraction data were collected to resolutions of 2.0 and 1.95 A, respectively.

SUBMITTER: Zeytuni N

PROVIDER: S-EPMC2898471 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature

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Crystallization and preliminary crystallographic analysis of the Magnetospirillum magneticum AMB-1 and M. gryphiswaldense MSR-1 magnetosome-associated proteins MamA.

Zeytuni Natalie N Zarivach Raz R

Acta crystallographica. Section F, Structural biology and crystallization communications 20100624 Pt 7

MamA is a unique magnetosome-associated protein that is predicted to contain six sequential tetratricopeptide-repeat (TPR) motifs. The TPR structural motif serves as a template for protein-protein interactions and mediates the assembly of multi-protein complexes. Here, the crystallization and preliminary X-ray analysis of recombinant and purified Magnetospirillum magneticum and M. gryphiswaldense MamA are reported for the first time. M. gryphiswaldense MamADelta41 crystallized in the tetragonal ...[more]

PMID: 20606283

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Project description:The bacterium Magnetospirillum gryphiswaldense MSR-1 forms nanosized membrane-enclosed organelles termed magnetosomes. The mamXY operon, part of the magnetosome island (MAI), includes the mamY, mamX, mamZ, and ftsZ-like genes, which initiate gene transcription via the same promoter. We used a combination of molecular biological techniques (targeting of cross-linking reagents) and high-resolution mass spectrometry to investigate the coordinated activity of the four MamXY proteins in magnetite biomineralization. The FtsZ-like protein was shown by confocal laser scanning microscopy to be dispersed in the cytoplasm in the early stage of cell growth and then gradually polymerized along the magnetosome chain. Interactions of various pairs of MamXY proteins were observed using a bacterial two-hybrid system. We constructed a recombinant FtsZ-like-overexpressing strain, examined its growth patterns, and extracted magnetosome membrane proteins using a modified SDS/boiling method with BS2G-d0/d4 reagent, which helped stabilize interactions among MamXY proteins. In liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis, MamY expression was detected first and remained highest among the four proteins throughout all stages of cell growth. MamX and MamZ expression was detected subsequently. The four proteins displayed coordinated expression patterns during the magnetosome maturation process. Unique peptides discovered in the MamXY protein sequences appeared to constitute "hidden" interaction sites involved in the formation of MamXY complex that helped control magnetosome shape and size.IMPORTANCE mamXY operon genes play an essential role in magnetite biomineralization, participate in redox reactions, and control magnetosome shape and size. However, mechanisms whereby the four MamXY proteins function together in iron oxidoreduction and transport are poorly understood. We used a combination of targeted cross-linking techniques and high-resolution mass spectrometry to elucidate the coordinated activity patterns of the MamXY proteins during magnetite biomineralization. Our findings indicate that the FtsZ-like protein undergoes polymerization and then recruits MamY, MamX, and MamZ in turn, and that these interactions depend on unique peptides present in the protein sequences. A hypothetical model of the functionalities of these proteins is proposed that accounts for the findings and provides a basis for further studies of coordination among magnetosome island (MAI) gene clusters during the process of magnetosome formation.

Dataset Information

Crystallization and preliminary crystallographic analysis of the Magnetospirillum magneticum AMB-1 and M. gryphiswaldense MSR-1 magnetosome-associated proteins MamA.

Publications

Crystallization and preliminary crystallographic analysis of the Magnetospirillum magneticum AMB-1 and M. gryphiswaldense MSR-1 magnetosome-associated proteins MamA.

Similar Datasets

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