Experimental Cell Research Volume 286, Issue 1 , 15 May 2003, Pages 12-21
Petra Skare (a)(1), Jan-Peter Kreivi (b)(1), Åsa Bergström (a)(2) and Roger Karlsson (a)
(a) Department of Cell Biology, The Wenner-Gren Institute, Stockholm University, SE-106 91, Stockholm, Sweden
(b) Department of Medical Biochemistry and Microbiology, Uppsala University, BMC Box 582, SE-751 23, Uppsala, Sweden
Received 30 July 2002; revised 11 December 2002. Available online 2 April 2003.
(1) These authors contributed equally.
(2) Present address: Gnothis AB, Kistagången 16, SE-64 40 Kista, Sweden.
Abstract
Profilin is one of the major components controlling actin polymerization. Here, profilin I was located in fibroblasts and HeLa cells by the use of two different sets of affinity-purified antibodies. Both antibody preparations labeled nuclei in a speckle-like pattern and displayed extensive colocalization with small nuclear ribonucleoprotein particle (snRNP)-core proteins and p80 coilin-containing Cajal bodies. Treatment with actinomycin D led to largely similar reorganizations of snRNPs and profilin, while profilin and Cajal bodies separated under these conditions. One of the profilin antibodies interfered with pre-mRNA splicing in vitro, further indicating a role for profilin during pre-mRNA processing.
Author Keywords: Profilin; Nuclear distribution; Pre-mRNA splicing; Sm proteins
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