ABCC1 p.Lys31Ala

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PMID: 22362766 [PubMed] Netz DJ et al: "A bridging [4Fe-4S] cluster and nucleotide binding are essential for function of the Cfd1-Nbp35 complex as a scaffold in iron-sulfur protein maturation."
No. Sentence Comment
259 First, yeast cells bearing only the Walker A-mutated Cfd1 (K31A) or Nbp35 (K86A), generated by plasmid FIGURE 6.
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ABCC1 p.Lys31Ala 22362766:259:59
status: NEW
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312 C, 55 Fe incorporation into plasmid-encoded Cfd1-TAP or its K31A mutant version was measured in Gal-CFD1 cells grown in galactose- or glucose-containing minimal medium as indicated.
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ABCC1 p.Lys31Ala 22362766:312:60
status: NEW
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311 C, 55 Fe incorporation into plasmid-encoded Cfd1-TAP or its K31A mutant version was measured in Gal-CFD1 cells grown in galactose- or glucose-containing minimal medium as indicated.
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ABCC1 p.Lys31Ala 22362766:311:60
status: NEW
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PMID: 26195633 [PubMed] Camire EJ et al: "The Yeast Nbp35-Cfd1 Cytosolic Iron-Sulfur Cluster Scaffold Is an ATPase."
No. Sentence Comment
138 Lane 1, His Nbp35; lane 2, His Cfd1; lane 3, Nbp35-Cfd1 complex; lane 4, Nbp35-K26A Cfd1; lane 5, Nbp35-K31A Cfd1; lane 6, K86A Nbp35-Cfd1.
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ABCC1 p.Lys31Ala 26195633:138:104
status: NEW
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150 The lysine mutants K86A Nbp35-Cfd1, Nbp35-K26A Cfd1, and Nbp35-K31A Cfd1 were expressed at similar levels as the wild-type Nbp35-Cfd1 complex, whereas little K81A Nbp35 was present in crude extracts upon co-expression with wild-type Cfd1.
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ABCC1 p.Lys31Ala 26195633:150:63
status: NEW
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151 For the remaining three mutants, intact complexes containing K86A Nbp35-Cfd1, Nbp35-K26A Cfd1, and Nbp35-K31A Cfd1 could be obtained.
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ABCC1 p.Lys31Ala 26195633:151:105
status: NEW
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154 To confirm via a second independent method that our mutations did not significantly affect the structure of the heterocomplex, we analyzed the secondary structure content of the two canonical lysine mutants, K86A Nbp35-Cfd1 and Nbp35-K31A Cfd1, via CD.
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ABCC1 p.Lys31Ala 26195633:154:234
status: NEW
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202 C shows wild-type Nbp35-Cfd1 complex (afb;), Nbp35-K26A Cfd1 (˜); Nbp35-K31A Cfd1(Éa;), and Nbp35-D55A Cfd1 (E).
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ABCC1 p.Lys31Ala 26195633:202:80
status: NEW
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220 We found that mutation of either lysine in the Walker A motif, K26A or K31A, resulted in decreased ATP hydrolysis activity of the Nbp35-Cfd1 complex (Fig. 5C, triangles).
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ABCC1 p.Lys31Ala 26195633:220:71
status: NEW
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