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. 2000 Feb 7;148(3):405–416. doi: 10.1083/jcb.148.3.405

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© 2000 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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HsCen3p interacts with Kar1p extracts of yeast cells overexpressing HsCen3p, Cdc31p. HsCen3p in a Δkar1/cdc31-16 background, or HsCen2p were immunoprecipitated with anti-HsCen3p affinity-purified antibodies or with anti-HsCen2p antibodies. Immunoprecipitated proteins were separated on SDS-PAGE, transferred onto nitrocellulose, and revealed with anti-HsCen3p, anti-Cdc31p, or anti-Kar1p antibodies, or with anti-HsCen2p and anti-Kar1p antibodies. In cells overexpressing HsCen3p, HsCen3p and Kar1p are coimmunoprecipitated. It is noteworthy that in the conditions we have used, Cdc31p and Kar1p are not coimmunoprecipitated, whereas HsCen2p and Kar1p are.