Molecular Characterization of a novel, Repetitve Protein of the Paraflagellar Rod in Trypanosoma-Brucei

Woodward, Robert and Carden, Martin J. and Gull, Keith (1994) Molecular Characterization of a novel, Repetitve Protein of the Paraflagellar Rod in Trypanosoma-Brucei. Molecular and Biochemical Parasitology, 67 (1). pp. 31-39. ISSN 0166-6851. (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1016/0166-6851(94)90093-0

Abstract

A partial cDNA clone, termed 5.20, was isolated from a lambda-gt11 phage expression library using a complex antiserum to the T. brucei cytoskeleton. Antisera against the fusion protein product of this 5.20 cDNA recognized a closely-spaced polypeptide doublet of high molecular weight (ca. 180-200 kDa) on immunoblots of T. brucei cytoskeletal preparations. Immunogold labelling suggested the 5.20 protein is intracellular and localized along the entire length of the paraflagellar rod. This pattern is similar to that generated with a monoclonal antibody, ROD1, which recognizes a high molecular weight protein doublet indistinguishable from that detected by 5.20-specific antisera. ROD1 recognizes mammalian spectrin, but the use of specific anti-spectrin antibodies for immunoblotting did not support ideas that 5.20 encodes spectrin or that spectrin can be specifically detected in T. brucei by such methods. Moreover, the sequence of the 5.20 cDNA insert bears little similarity, either in its nucleotide or predicted amino acid sequence to other known proteins and appears to be a unique cytoskeletal protein characterized especially by sequential amino acid sequence repetitiveness. The location of this novel protein suggests it may be responsible for providing either paraflagellar rod-membrane links or for organizing the more abundant paraflagellar rod structural proteins.

Item Type: Article
Uncontrolled keywords: TRYPANOSOME; CDNA; PARAFLAGELLAR ROD; CYTOSKELETON
Subjects: Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: P. Ogbuji
Date Deposited: 09 Jun 2009 13:52
Last Modified: 08 Jul 2014 14:12
Resource URI: http://kar.kent.ac.uk/id/eprint/20111 (The current URI for this page, for reference purposes)
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