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Molecular and Cellular Biology, August 2002, p. 5859-5868, Vol. 22, No. 16
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.16.5859-5868.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Interactions between Telomerase and Primase Physically Link the Telomere and Chromosome Replication Machinery

Saugata Ray,1 Zemfira Karamysheva,2 Libin Wang,2 Dorothy E. Shippen,2 and Carolyn M. Price3*

Department of Pediatrics, University of California, San Diego School of Medicine, La Jolla, California 92093-0627,1 Department of Biochemistry & Biophysics, Texas A&M University, College Station, Texas 77843-2128,2 Department of Molecular Genetics, Biochemistry & Microbiology, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267-05243

Received 1 April 2002/ Returned for modification 30 April 2002/ Accepted 9 May 2002

In the ciliate Euplotes crassus, millions of new telomeres are synthesized by telomerase and polymerase {alpha}-primase during macronuclear development in mated cells. Concomitant with de novo telomere formation, telomerase assembles into higher-order complexes of 550 kDa, 1,600 kDa, and 5 MDa. We show here that telomerase is physically associated with the lagging-strand replication machinery in these complexes. Antibodies against DNA primase precipitated telomerase activity from all three complexes from mated cells but not the 280-kDa telomerase complex from vegetatively growing cells. Moreover, when telomerase was affinity purified, primase copurified with enzyme from mated cells but not with the 280-kDa vegetative complex. Thus, the association of telomerase and primase is developmentally regulated. Intriguingly, PCNA (proliferating cell nuclear antigen) was also found in the 5-MDa complex from mated cells. We therefore speculate that this complex is a complete telomere synthesis machine, while the smaller complexes are assembly intermediates. The physical association of telomerase and primase explains the coordinate regulation of telomeric G- and C-strand synthesis and the efficiency of telomere addition in E. crassus.

* Corresponding author. Mailing address: Department of Molecular Genetics, Biochemistry & Microbiology, College of Medicine, University of Cincinnati, ML 0524, 231 Albert Sabin Way, Cincinnati, OH 45267. Phone: (513) 558-0450. Fax: (513) 558-8474. E-mail: Carolyn.Price{at}uc.edu.

Molecular and Cellular Biology, August 2002, p. 5859-5868, Vol. 22, No. 16
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.16.5859-5868.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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