Difference between revisions of "Part:BBa K590016"

Revision as of 20:15, 28 September 2011

sfGFP_mamI_pGA1C3

This part was made by [http://2011.igem.org/Team:Washington UW iGEM Team 2011] and was contributed to the [http://2011.igem.org/Team:Washington/Magnetosomes/Results Magnetosome Toolkit].

Usage and Biology

This part consists of the mamI gene from Magnetospirillum magneticum strain AMB-1, fused to superfolder gfp cloned into pGA1C3. MamI is a membrane-localized protein that is essential for magnetosome vesicle formation, and is also known to bind the MamK filament. Since it localizes to the membrane, MamI may be useful in maximizing the flux of biosynthetic pathways as a membrane-linker protein.

We transformed this part into a E. coli BL-21 lacI^q strain and observed strong membrane localization.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
INCOMPATIBLE WITH RFC[1000]
Illegal SapI.rc site found at 80

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 ===Usage and Biology===
-This part consists of the <i>mamI</i> gene from <i>Magnetospirillum magneticum</i> strain AMB-1, fused to  superfolder <i>gfp</i> cloned into [https://parts.igem.org/wiki/index.php?title=Part:BBa_K590011 pGA1C3]. MamI is a membrane-localized protein that is essential for magnetosome vesicle formation, and is also known to bind the MamK filament. Since it localizes to the membrane, MamI may be useful in maximizing the flux of biosynthetic pathways as a membrane-linker protein.
+This part consists of the <i>mamI</i> gene from <i>Magnetospirillum magneticum</i> strain AMB-1, fused to  superfolder <i>gfp</i> cloned into [https://parts.igem.org/wiki/index.php?title=Part:BBa_K590011 pGA1C3]. MamI is a membrane-localized protein that is essential for magnetosome vesicle formation, and is also known to bind the [https://parts.igem.org/wiki/index.php?title=Part:BBa_K590015 MamK] filament. Since it localizes to the membrane, MamI may be useful in maximizing the flux of biosynthetic pathways as a membrane-linker protein.
 We transformed this part into a ''E. coli'' BL-21 lacI<sup>q</sup> strain and observed strong membrane localization.