BBa_K1954004
1
BBa_K1954004
Mutacin III biosynthetic device
2016-10-16T11:00:00Z
2016-10-19T02:13:09Z
Our device was based on the sequence of AF154675.1
The biosynthetic locus was engineered by our team in a form allowing for high-yield and fine-tuned expression of mutacin III (Fig. 1). We placed a strong T7 promoter upstream of mutA to obtain high levels of the propeptide, a repressible pTet promoter upstream of the mutBCDP co-transcription unit and an inducible araBAD promoter for the mutT gene, coding for the ATP-binding-cassette-like transporter of mutacin III. All illegal restriction sites were removed from the endogenous sequences by silent mutagenesis.
Fig. 1. Simplified diagram of the mutacin III biosynthetic locus designed by UCL iGEM 2016.
Mutacin III is a ribosomally synthesized 22 amino acid screw-shaped lanthionine-containing peptide. The biosynthesis of mutacin III involves the expression of the structural gene mutA to make a prepropeptide, comprising a C-terminal propeptide and an N-terminal leader peptide from which the former undergoes processing and the latter is cleaved off before export into the medium (4). The specific post-translational modifications make mutacin III distinct from other bacteriocins and are introduced by enzymes coded for by other genes in the locus (mutBCDP). Basing on sequence homologies of genes in the locus with those of other lantibiotic biosynthetic loci it can be inferred that these enzymes catalyze the dehydration (mutB) and cyclization (mutC) of the propeptide serine and threonine residues which can condense with a neighboring cysteine residue (6) leading to the formation of lanthionine or methyllanthionine (thioether) bridges, respectively. The enzyme coded by mutD catalyzes the oxidative decarboxylation of the C-terminal cysteine residue (7) while the product of mutP is a serine protease which cleaves the leader peptide and is likely the last step in the biosynthesis (8). The mature mutacin III is composed of rings connected by flexible linkers (Fig. 2) which may be important in the mechanism of bacteriocidal activity (9). Following export, the peptide is believed to form transmembrane pores as monomer aggregates leading to membrane disruption and efflux of cellular components (10). The content of anionic phospholipids in the membrane has been suggested to be an important factor influencing initial binding ??? mutacin III has a net positive charge whereas Gram-positive bacteria have a high relative amount of anionic lipids (11).
Fig. 2. The structure of mature mutacin III (10).
In one investigation of the activity of mutacin-related lantibiotic gallidermin it became clear that lantibiotics are more effective in preventing biofilm formation rather than in exterminating microorganisms already embedded in biofilms (12). To reflect this, our device could be used to transform E. coli cells and employed as an anti-cariogenic strategy in replacement therapy (Fig. 3). Such a novel bacterial strain would demonstrate features of a successful effector strain as it would not cause disease by itself and because it could displace the host pathogenic bacteria. Importantly, there are very few existing examples of lantibiotic resistance compared with antibiotics and only one mechanism of resistance to mutacin III, known as CprRK in Clostridium difficile, has been established (13). Moreover, the fact that a closely related lantibiotic nisin has been shown to exhibit low in vivo toxicity levels (14) and has been widely used as food preservative from as early as mid 1940s (15) further encourages the prospect of considering the employment of mutacin III as an anti-cariogenic agent.
false
false
_2421_
24377
32880
9
false
All restriction sites were removed by silent mutagenesis.
false
Kamil Żmijewski, Luba Prout
annotation2515079
1
T7 promoter
range2515079
1
1179
1197
annotation2515085
1
muB
range2515085
1
1656
4626
annotation2515084
1
BBa_B0034
range2515084
1
1638
1649
annotation2515093
1
BBa_B1002
range2515093
1
9864
9897
annotation2515076
1
AraC
range2515076
1
129
1207
annotation2515090
1
BBa_I0500
range2515090
1
8022
8187
annotation2515081
1
BBa_B0034
range2515081
1
1220
1231
annotation2515073
1
TetR 2
range2515073
1
92
110
annotation2515089
1
rrnB T1
range2515089
1
7872
7943
annotation2515075
1
BBa_I0500
range2515075
1
129
1338
annotation2515067
1
-35
range2515067
1
4
9
annotation2515080
1
Pbad
range2515080
1
1208
1338
annotation2515066
1
BBa_I14033
range2515066
1
1
38
annotation2515070
1
mutR
range2515070
1
59
913
annotation2515074
1
-10
range2515074
1
109
114
annotation2515077
1
rrnB T1
range2515077
1
958
1029
annotation2515068
1
-10
range2515068
1
27
32
annotation2515086
1
mutC
range2515086
1
4615
5889
annotation2515072
1
-35
range2515072
1
86
91
annotation2515078
1
rrnB T2
range2515078
1
1121
1148
annotation2515091
1
BBa_B0034
range2515091
1
8205
8216
annotation2515069
1
BBa_B0034
range2515069
1
47
58
annotation2515087
1
mutD
range2515087
1
5913
6479
annotation2515071
1
TetR 1
range2515071
1
67
85
annotation2515083
1
T7 terminator
range2515083
1
1507
1554
annotation2515092
1
mutT
range2515092
1
8223
9848
annotation2515082
1
mutA
range2515082
1
1238
1429
annotation2515088
1
mutP
range2515088
1
6484
7827
BBa_K1954004_sequence
1
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igem2sbol
1
iGEM to SBOL conversion
Conversion of the iGEM parts registry to SBOL2.1
James Alastair McLaughlin
Chris J. Myers
2017-03-06T15:00:00.000Z