Journal: Fungal Biology and Biotechnology
Article Title: Selection markers for transformation of the sequenced reference monokaryon Okayama 7/#130 and homokaryon AmutBmut of Coprinopsis cinerea
doi: 10.1186/s40694-020-00105-0
Figure Lengend Snippet: Alignment of A. wt Pab1 from C. cinerea monokaryon OK130 ( Cc Pab1) with PabA ( Ec PabA, underlaid in yellow) and PabB of E. coli ( Ec PabB, underlaid in dusky pink) and B. wt Ade8 from C. cinerea strain AmutBmut ( Cc Ade8) with PurD ( Ec PurD, underlaid in yellow) and PurM of E. coli ( Ec PurM, underlaid in dusky pink), respectively. a The catalytic triad, glutamine binding residues and residues involved in ammonia tunnel formation in PabA are marked with red, green and blue symbols *, respectively. Other residues affecting enzymatic activities and bonding to PabB are marked with grey squares. The position of a stabilizing residue stretch called oxyanion hole is underlaid in light blue, a sequence stretch for chorismate signal transfer in olive [ , , ]. Red letters in PabB mark helical regions, blue letters β-sheets. The conserved PIKGT motif, sequences for interaction with PabA, for signal transfer of chorismate binding, and of a binding pocket for tryptophan implicated in structural stabilization are underlaid in olive, bright yellow, grey and light blue, respectively. The residue K in the PIKGT motif which is mutated in C. cinerea AmutBmut (K546E) is marked in red. Symbols * in red and black mark (predicted) active site residues and Mg 2+ -binding residues in two chorismate-interacting helices, respectively. Triangles in black indicate residues that contact the bound tryptophan and grey squares further residues where mutations affect functionality [ – , ]. b Red, blue, green and magenta letters mark the N, B, A, and C domains of PurD. The positions of the P-loop and the flexible A and B loops in PurD are underlaid in light blue, olive and orange, respectively. Symbols * in black, red, and blue mark residues that recognize the adenine base, ribose and phosphate of the nucleotide, whereas grey squares indicate residues interacting with the ligand PRA [ , ]. The residue N in the A loop which is mutated in C. cinerea OK130 (N231D) is marked in red. In PurM, symbols * mark (predicted) nucleotide binding residues and triangles (in grey predicted) binding sites of the substrate N -formylglycinamidine ribonucleotide (FGAM)
Article Snippet: Monokaryons Okayama 7/#130 (short name in literature OK130 [ ]; ATCC MYA-4618, FGSC 9003; genotype: A43 , B43 , ade8-1 ), FA2222 (DSM 28333; A5 , B6 , acu1 , trp1.1,1.6 [ ]) and PG78 (DSM 28337; A6 , B42 , pab1-1 , trp1.1,1.6 [ ]), and the self-fertile homokaryon AmutBmut (FGSC 25122; genotype: A43mut , B43mut , pab1-1 [ ]) were routinely cultivated on YMG/T medium at 37 °C [ ].
Techniques: Binding Assay, Sequencing
ATCC is a verified supplier 
ATCC manufactures this product 
![Alignment of A. wt Pab1 from C. cinerea monokaryon <t>OK130</t> ( Cc Pab1) with PabA ( Ec PabA, underlaid in yellow) and PabB of E. coli ( Ec PabB, underlaid in dusky pink) and B. wt Ade8 from C. cinerea strain AmutBmut ( Cc Ade8) with PurD ( Ec PurD, underlaid in yellow) and PurM of E. coli ( Ec PurM, underlaid in dusky pink), respectively. a The catalytic triad, glutamine binding residues and residues involved in ammonia tunnel formation in PabA are marked with red, green and blue symbols *, respectively. Other residues affecting enzymatic activities and bonding to PabB are marked with grey squares. The position of a stabilizing residue stretch called oxyanion hole is underlaid in light blue, a sequence stretch for chorismate signal transfer in olive [ , , ]. Red letters in PabB mark helical regions, blue letters β-sheets. The conserved PIKGT motif, sequences for interaction with PabA, for signal transfer of chorismate binding, and of a binding pocket for tryptophan implicated in structural stabilization are underlaid in olive, bright yellow, grey and light blue, respectively. The residue K in the PIKGT motif which is mutated in C. cinerea AmutBmut (K546E) is marked in red. Symbols * in red and black mark (predicted) active site residues and Mg 2+ -binding residues in two chorismate-interacting helices, respectively. Triangles in black indicate residues that contact the bound tryptophan and grey squares further residues where mutations affect functionality [ – , ]. b Red, blue, green and magenta letters mark the N, B, A, and C domains of PurD. The positions of the P-loop and the flexible A and B loops in PurD are underlaid in light blue, olive and orange, respectively. Symbols * in black, red, and blue mark residues that recognize the adenine base, ribose and phosphate of the nucleotide, whereas grey squares indicate residues interacting with the ligand PRA [ , ]. The residue N in the A loop which is mutated in C. cinerea OK130 (N231D) is marked in red. In PurM, symbols * mark (predicted) nucleotide binding residues and triangles (in grey predicted) binding sites of the substrate N -formylglycinamidine ribonucleotide (FGAM)](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_2465/pmc07552465/pmc07552465__40694_2020_105_Fig1a_HTML.jpg)
