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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.
Each MAGP was examined for its distribution relative to operons in the 169 bacteria.
In summary, gene co-transcription and known protein physical interaction together could explain two thirds of the non-ribosomal MAGP.
We then examined each MAGP to see if the two genes were functionally coupled (see details in Additional file 6).
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MAGP-2 can also interact with αvβ3 integrins via a RGD sequence that is not found in MAGP-1.
The microfibril-associated glycoproteins MAGP-1 and MAGP-2 are extracellular matrix proteins that interact with fibrillin to influence microfibril function.
Morpholino knockdown of MAGP-1 expression in zebrafish resulted in abnormal vessel wall architecture and altered vascular network formation.
Inactivation of the gene for MAGP-2 in mice produced a neutropenia yet had minimal effects on bone or adipose homeostasis.
Loss of MAGP-1 around the hair follicle/pore areas was also observed, suggesting a possible correlation between MAGP-1 loss and enlarged pores in aged skin.
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