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© The Rockefeller University Press, 0021-9525/1998//321 $5.00
The Journal of Cell Biology, Volume 141, Number 2, , 1998 321-333

Articles

Human Autoantibodies Reveal Titin as a Chromosomal Protein



Cristina Machado*,{ddagger}, Claudio E. Sunkel{ddagger},§, and Deborah J. Andrew*

* Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205-2196; {ddagger} Laboratório de Genética Molecular, Instituto de Biologia Molecular e Celular, 4150 Porto, Portugal; and § Departamento de Biologia Molecular, Instituto de Ciências Biomédicas Abel Salazar, Universidade do Porto, 4050 Porto, Portugal

Assembly of the higher-order structure of mitotic chromosomes is a prerequisite for proper chromosome condensation, segregation and integrity. Understanding the details of this process has been limited because very few proteins involved in the assembly of chromosome structure have been discovered. Using a human autoimmune scleroderma serum that identifies a chromosomal protein in human cells and Drosophila embryos, we cloned the corresponding Drosophila gene that encodes the homologue of vertebrate titin based on protein size, sequence similarity, developmental expression and subcellular localization. Titin is a giant sarcomeric protein responsible for the elasticity of striated muscle that may also function as a molecular scaffold for myofibrillar assembly. Molecular analysis and immunostaining with antibodies to multiple titin epitopes indicates that the chromosomal and muscle forms of titin may vary in their NH2 termini. The identification of titin as a chromosomal component provides a molecular basis for chromosome structure and elasticity.

Abbreviations used in this paper: E, glutamic acid; FN3, fibronectin type III; K, lysine; MG, myasthenia gravis; MIR, major immunogenic region; ORF, open reading frame; P, proline; V, valine.

C. Machado was supported by a Ph.D. fellowship from Junta Nacional de Investigação Cientifica e Tecnológica (JNICT) and, in part, by grants from Fundação Luso-Americana para o Desenvolvimento and Fundação Calouste Gulbenkian. This work was supported by a grant from the Council for Tobacco Research to D.J. Andrew and a grant from JNICT to C.E. Sunkel.

Address all correspondence to Deborah J. Andrew, Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, Maryland 21205-2196. Tel.: (410) 614-2722. Fax: (410) 955-4129. E-mail: debbie_andrew{at}qmail.bs.jhu.edu


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