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

. 1997 Aug 11;138(3):575–588. doi: 10.1083/jcb.138.3.575

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

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/).

PMC Copyright notice

Actin binding to GST–abLIM fusion proteins. Three different polypeptides expressed in E. coli and purified by affinity chromatography were tested for the ability to associate with F-actin: GST only (GST), GST fused to part of the dematin region of abLIM (GST–dem), and GST fused to part of the LIM domain of abLIM (GST–LIM). Each polypeptide was incubated with (+actin) or without (−actin) actin under conditions that favor actin polymerization. After centrifugation to sediment F-actin, each sample was separated into a supernatant (S) and pellet (P). Samples are indicated at the top of the SDS gel. Control incubations with actin but without added fusion proteins were run in parallel (far right panel). Mobilities of each fusion protein with the appropriate mass are indicated by filled arrowheads (right). Note the presence of each fusion protein in the supernatant fraction in −actin samples (left). Only GST–dem is enriched in the +actin pellet fraction, indicating cosedimentation of GST–dem, but not GST or GST–LIM, with F-actin.