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. 1999 Nov 15;147(4):761–774. doi: 10.1083/jcb.147.4.761

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© 1999 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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graphic file with name JCB9908104.f3a.jpg — The COOH-terminal domain of PEX12 interacts with the COOH-terminal domain of PEX10 in the yeast two-hybrid system. Two-hybrid reporter strains expressing the indicated fusion proteins were transferred to a nitrocellulose filter, submerged in liquid nitrogen to lyse the cells, and assayed for β-galactosidase activity. AD, GAL4 activation domain; and BD, GAL4-binding domain. (B) PEX10 binds immobilized PEX12C in vitro. 10 μg of purified MBP-LacZα and purified MBP-PEX12C were resolved by SDS-PAGE, transferred to membranes, and probed with ³⁵S-labeled PEX10 (upper panel). A duplicate gel was stained before transfer with Coomassie blue (lower panel). (C) Coimmunoprecipitation of PEX10 with PEX12. Lysates from cells cotransfected with either pcDNA3-PEX12 and pcDNA3-PEX10/3xHA (left lane) or pcDNA3-PEX12/3xmyc and pcDNA3-PEX10/3xHA (right lane) were immunoprecipitated with anti–myc antibodies and analyzed by immunoblot with anti–HA antibodies. Aliquots of the crude lysates before immunoprecipitation were also assayed for PEX10/3xHA levels by immunoblot.

graphic file with name JCB9908104.f3bc.jpg — The COOH-terminal domain of PEX12 interacts with the COOH-terminal domain of PEX10 in the yeast two-hybrid system. Two-hybrid reporter strains expressing the indicated fusion proteins were transferred to a nitrocellulose filter, submerged in liquid nitrogen to lyse the cells, and assayed for β-galactosidase activity. AD, GAL4 activation domain; and BD, GAL4-binding domain. (B) PEX10 binds immobilized PEX12C in vitro. 10 μg of purified MBP-LacZα and purified MBP-PEX12C were resolved by SDS-PAGE, transferred to membranes, and probed with ³⁵S-labeled PEX10 (upper panel). A duplicate gel was stained before transfer with Coomassie blue (lower panel). (C) Coimmunoprecipitation of PEX10 with PEX12. Lysates from cells cotransfected with either pcDNA3-PEX12 and pcDNA3-PEX10/3xHA (left lane) or pcDNA3-PEX12/3xmyc and pcDNA3-PEX10/3xHA (right lane) were immunoprecipitated with anti–myc antibodies and analyzed by immunoblot with anti–HA antibodies. Aliquots of the crude lysates before immunoprecipitation were also assayed for PEX10/3xHA levels by immunoblot.