Article Abstract:
The crystal structure of a Hedgehog protein (Hh) is studied to identify the mechanisms involved in its autoprocessing and relationship with self-splicing proteins which interact with Drosophila Hedgehog protein (Hh-C). Results show that the crystal structure of a 17 kDa fragment of Hh-C builds up a relationship with the self-splicing proteins which helped identify active site residues. The residues were mutated and became a contributing factor to thioester formation and cholesterol transfer.
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Article Abstract:
The autoprocessing reaction is shown to proceed via an internal thioester intermediate and result in a covalent modification that increases the signaling domain's hydrophobic character and influences its subcellular and spatial distribution. Truncated unprocessed amino-terminal protein is shown to cause embryonic mispatterning even when expression is localized to cells that normally express Hh. This suggests the role of autoprocessing in the spatial regulation of hh signaling.
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Article Abstract:
In vivo studies indicate the presence of a single conserved signalling pathway for both local and direct long-range inductions of hedgehog proteins. The amino-terminal cleavage product(SHH-N) of the sonic hegehog gene causes the long-range sclerotome induction and dermomyotome repression in somite differentiation by the notochord. Increased activity of cyclic AMP-dependent protein kinase A decreases the activity of SHH-N.
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