ABCC8 p.Glu88Ala

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PMID: 9643548 [PubMed] Poncelet M et al: "Targeted deletion and mutational analysis of the essential (2Fe-2S) plant-like ferredoxin in Synechocystis PCC6803 by plasmid shuffling."
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).
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ABCC8 p.Glu88Ala 9643548:100:113
status: NEW
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107 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.
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ABCC8 p.Glu88Ala 9643548:107:15
status: NEW
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133 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).
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ABCC8 p.Glu88Ala 9643548:133:35
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158 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.
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ABCC8 p.Glu88Ala 9643548:158:105
status: NEW
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PMID: 11687213 [PubMed] Setif P et al: "Ferredoxin and flavodoxin reduction by photosystem I."
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).
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ABCC8 p.Glu88Ala 11687213:393:36
status: NEW
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