ABCD1 p.Arg452Glu
| Predicted by SNAP2: | A: N (87%), C: N (93%), D: N (78%), E: N (93%), F: N (72%), G: N (78%), H: N (97%), I: N (82%), K: N (97%), L: N (87%), M: N (87%), N: N (93%), P: N (78%), Q: N (97%), S: N (93%), T: N (93%), V: N (87%), W: D (59%), Y: N (78%), |
| Predicted by PROVEAN: | A: N, C: N, D: N, E: N, F: N, G: N, H: N, I: N, K: N, L: N, M: N, N: N, P: N, Q: N, S: N, T: N, V: N, W: N, Y: N, |
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[hide] Identification of in vivo substrates of the chaper... Biosci Biotechnol Biochem. 2007 Apr;71(4):1073-7. Epub 2007 Apr 7. Endo A, Kurusu Y
Identification of in vivo substrates of the chaperonin GroEL from Bacillus subtilis.
Biosci Biotechnol Biochem. 2007 Apr;71(4):1073-7. Epub 2007 Apr 7., [PMID:17420574]
Abstract [show]
We investigated GroEL substrates from Bacillus subtilis 168 using the single-ring mutant of B. subtilis GroEL. We identified 28 candidates for GroEL substrates, of which Spo0B, Ald, Eno, SpoIIP, and FbaA were involved in spore formation, and Rnc, Tuf, Eno, Tsf, and FbaA were essential for B. subtilis growth. As observed at the protein level, the amount of SpoIIP interaction with GroEL increased at 3 h after initiation of sporulation.
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No. Sentence Comment
11 This mutant has four amino acid substitutions (R452E, E461A, S463A, and V464A, in E. coli GroEL) that prevent the formation of a double-ring structure and the release of GroES,7) and hence substrates can be observed to accumulate in the closed folding cage formed by the molecule.
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ABCD1 p.Arg452Glu 17420574:11:47
status: NEW