ABCC8 p.Glu88Ala
| Predicted by SNAP2: | A: N (66%), C: D (59%), D: N (78%), F: D (71%), G: D (59%), H: D (66%), I: N (78%), K: D (53%), L: D (59%), M: D (63%), N: D (63%), P: D (80%), Q: N (66%), R: D (75%), S: N (72%), T: N (61%), V: D (53%), W: D (75%), Y: D (71%), |
| Predicted by PROVEAN: | A: N, C: D, D: N, F: D, G: D, H: N, I: D, K: N, L: D, M: D, N: N, P: D, Q: N, R: N, S: N, T: D, V: D, W: D, Y: D, |
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[hide] Targeted deletion and mutational analysis of the e... Mol Microbiol. 1998 May;28(4):813-21. Poncelet M, Cassier-Chauvat C, Leschelle X, Bottin H, Chauvat F
Targeted deletion and mutational analysis of the essential (2Fe-2S) plant-like ferredoxin in Synechocystis PCC6803 by plasmid shuffling.
Mol Microbiol. 1998 May;28(4):813-21., [PMID:9643548]
Abstract [show]
The genes encoding (2Fe-2S) plant-like ferredoxins were studied in the widely used cyanobacterium Synechocystis PCC6803. The fedl gene (ssI0020) coding for the most abundant ferredoxin product was found to be expressed strongly as a light-induced monocistronic transcript, whereas the other fed genes appeared to be silent (sIr1828) or moderately expressed as polycistronic transcripts regulated by either light fluence (sIr0150, negative control) or glucose availability (sII1382). fedl was found to be critical to Synechocystis PCC6803 viability in spite of sIr0150, sII1382 or flavodoxin induction, even after the addition of glucose that compensates for the loss of photosynthesis. Nevertheless, fedl could be deleted from all chromosome copies in cells propagating a fedl gene (even of heterologous origin) on a replicating plasmid. This strain was used as the host for the subsequent introduction of fedl mutant alleles propagated on a second vector. Analysis of the fedl mutant strains generated after plasmid exchange showed that the C18-C85 disulphide bridge is not central either to the tight compaction of ferredoxin I or to its reduction by photosystem I and demonstrated that the length of the Fedl carboxy terminus is important for effective PSI/FedI interactions. The plasmid-shuffling strategy presently described has general applicability for mutational analysis of essential genes in many organisms, as it is based on promiscuous plasmids.
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No. Sentence Comment
100 Three of the fedI mutant alleles presently tested encoded a protein with a single amino acid substitution (C85V, E88A or E93A), whereas the last one, originating from a PCR artifact, directed the synthesis of a FedI product with a C-terminal extension (KGNLSSLA).
X
ABCC8 p.Glu88Ala 9643548:100:113
status: NEW107 Similarly, the E88A mutant ferredoxin (pMP3 plasmid) behaved essentially as the wild-type protein, ruling out the contribution of E-88 to an important electrostatic interaction with PSI.
X
ABCC8 p.Glu88Ala 9643548:107:15
status: NEW133 We have found that the independent E88A and E93A mutations of fedI, each removing one negative charge, had little effect on the tested properties of ferredoxin (electrophoretic mobility, reduction by PSI).
X
ABCC8 p.Glu88Ala 9643548:133:35
status: NEW158 Similarly, the mutant alleles of the Synechocystis fedI gene carrying the amino acid substitutions C85V, E88A and E93A were synthesized by PCR, using the NdeI creating primer and any of the following XhoI mutagenic primers 5Ј-CCCA- TGGCCACTCGAGTTACCCTTAGTAGAGGTCTTCTTC-3Ј, 5Ј-CCCATGGCCACTCGAGTTACCCTTAGTAGAGGTCTG- CTTCTTTGTG-3Ј or 5Ј-CCATGGCCACTCGAGTTACCCT- TAGTAGAGGTCTTCTTCTTGTGGGTTGCAATGG-3Ј, as required.
X
ABCC8 p.Glu88Ala 9643548:158:105
status: NEW[hide] Ferredoxin and flavodoxin reduction by photosystem... Biochim Biophys Acta. 2001 Oct 30;1507(1-3):161-79. Setif P
Ferredoxin and flavodoxin reduction by photosystem I.
Biochim Biophys Acta. 2001 Oct 30;1507(1-3):161-79., [PMID:11687213]
Abstract [show]
Ferredoxin and flavodoxin are soluble proteins which are reduced by the terminal electron acceptors of photosystem I. The kinetics of ferredoxin (flavodoxin) photoreduction are discussed in detail, together with the last steps of intramolecular photosystem I electron transfer which precede ferredoxin (flavodoxin) reduction. The present knowledge concerning the photosystem I docking site for ferredoxin and flavodoxin is described in the second part of the review.
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No. Sentence Comment
393 No change was observed for C85V and E88A mutants ([41]; C85, which is not highly conserved, is putatively involved in a disul'de bridge in Fd from Synechocystis 6803 [88]; an acidic residue is not fully conserved at position 88).
X
ABCC8 p.Glu88Ala 11687213:393:36
status: NEW