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. 1998 Feb 9;140(3):499–509. doi: 10.1083/jcb.140.3.499

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SUMO-1–modified RanGAP1 binds to a COOH-terminal region of Nup358, between Ran-binding domains three and four. (A) Schematic representation of Nup358. RBD, Ran-binding domain; CycH, cyclophilin homologous domain. Long vertical lines indicate FXFG repeats, and short vertical lines indicate FG repeats. Fragments that were found to bind modified RanGAP1 are indicated, as well as a summary of their binding activity (+, weak binding; ++, strong binding). Internal direct repeats in the RanGAP1-binding domain are indicated by open boxes. (B) Full-length RanGAP1 (lane 1) and COOH-terminal regions of RanGAP1 from amino acids 420–589 (NΔ419; lane 6) and 471– 589 (NΔ470; lane 11) were translated in vitro in the presence of [³⁵S]methionine. Translated proteins were assayed for binding to the domains of Nup358 indicated in A, as described in Materials and Methods. Molecular mass standards are indicated on the left, and asterisks denote SUMO-1–modified proteins.

SUMO-1–modified RanGAP1 binds to a COOH-terminal region of Nup358, between Ran-binding domains three and four. (A) Schematic representation of Nup358. RBD, Ran-binding domain; CycH, cyclophilin homologous domain. Long vertical lines indicate FXFG repeats, and short vertical lines indicate FG repeats. Fragments that were found to bind modified RanGAP1 are indicated, as well as a summary of their binding activity (+, weak binding; ++, strong binding). Internal direct repeats in the RanGAP1-binding domain are indicated by open boxes. (B) Full-length RanGAP1 (lane 1) and COOH-terminal regions of RanGAP1 from amino acids 420–589 (NΔ419; lane 6) and 471– 589 (NΔ470; lane 11) were translated in vitro in the presence of [³⁵S]methionine. Translated proteins were assayed for binding to the domains of Nup358 indicated in A, as described in Materials and Methods. Molecular mass standards are indicated on the left, and asterisks denote SUMO-1–modified proteins.