Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2015 Oct 1;26(19):3480–3488. doi: 10.1091/mbc.E15-05-0259

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2015 Ogi, Goto, Ghosh, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

“ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.

PMC Copyright notice

FIGURE 6: — Effect of tel1-21 or tel1-ΔC mutation on protein kinase activity in vitro. (A) Effect of tel1-21 or tel1-∆C mutation on Rad53 phosphorylation and Tel1 autophosphorylation. Extracts were prepared from cells expressing Tel1-HA (KSC1709), Tel1-KN-HA (KSC1751), Tel1-21-HA (KSC3087), or Tel1-ΔC-HA (KSC3549) and subjected to immunoprecipitation with anti-HA antibodies. Immunoprecipitates were assayed for kinase reactions using GST-Rad53 C-terminus as a substrate. Top, Rad53 phosphorylation and Tel1 autophosphorylation were detected by autoradiography, and the amount of Tel1 protein was analyzed by immunoblotting with anti-HA antibodies. Bottom, phosphoincorporation was normalized relative to that from wild-type Tel1 protein (100%). The average intensity calculated from three independent experiments is shown, and the error bars represent the SD derived from these experiments. (B) Tel1 autophosphorylation after incubation for various lengths of time. Tel1 proteins were immunoprecipitated and subjected to the in vitro kinase assay as in A, but the reaction mixtures were incubated for various lengths of time (0, 10, 20, and 40 min). Phosphoincorporation into Tel1 was normalized relative to that for wild-type Tel1 protein at 0 (0%) and 40 min (100%).