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Among those, 96 (85%) were accounted for by operons, and another 6 MAGP by physical protein interaction pairs.
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A mature mycolic acid is eventually transferred either to arabinogalactan (to form mAGP) in part by the Ag85 proteins, or to an α,α-trehalose-6-phosphate (T6P, leading to TMM) by an unknown mycolyltransferase [9].
To find out those MAGP not maintained by operon structures, we examined the genes from each MAGP in all the bacterial chromosomes.
Based on the proportion of bacteria in which the two genes belonged to the same operon, coupled with the distance between them in bacteria where they were not in the same operon (see Methods), we tested if a MAGP is maintained by operons.
This showed that 618 (58%) MAGP were composed of genes belonging to the same functional category, among which 391 were MAGP maintained by operons.
If in more than 50% of the bacteria, the two genes from a MAGP were coded in the same operon, we regarded this MAGP as maintained by the operon.
BY BLOOD, by Ellen Ullman.
We report herein the synthesis of hydrophilic hydrophilic AB diblock copolymers of 3-O-methacryloyl-d-galactopyranose (MAGP) with 2- dimethylamino)ethyl methacrylate (DMAEMA).
Just exterior to the cell membrane lies the mycolyl-arabinogalactan-peptidoglycan complex (mAGP).
The mycolic acids of these glycolipids are noncovalently intercolated with the mAGP.
However, only 127, i.e. 10.9%, of the 1164 interacting pairs are also MAGP, and conversely only 17.1% MAGP are interacting pairs in E. coli.
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