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Molecular and Cellular Biology, November 1998, p. 6641-6652, Vol. 18, No. 11
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Identification of a Novel Slow-Muscle-Fiber Enhancer Binding Protein, MusTRD1

John V. O'Mahoney,1 Kim L. Guven,1 Jia Lin,2 Josephine E. Joya,1 C. Stephen Robinson,1 Robert P. Wade,2 and Edna C. Hardeman1,*

Muscle Development Unit, Children's Medical Research Institute, Wentworthville, New South Wales 2145, Australia,1 and Department of Biological Chemistry, University of Maryland School of Medicine, Baltimore, Maryland 212012

Received 21 May 1998/Returned for modification 17 July 1998/Accepted 3 August 1998

The molecular mechanisms which are responsible for restricting skeletal muscle gene expression to specific fiber types, either slow or fast twitch, are unknown. As a first step toward defining the components which direct slow-fiber-specific gene expression, we identified the sequence elements of the human troponin I slow upstream enhancer (USE) that bind muscle nuclear proteins. These include an E-box, a MEF2 element, and two other elements, USE B1 and USE C1. In vivo analysis of a mutation that disrupts USE B1 binding activity suggested that the USE B1 element is essential for high-level expression in slow-twitch muscles. This mutation does not, however, abolish slow-fiber specificity. A similar analysis indicated that the USE C1 element may play only a minor role. We report the cloning of a novel human USE B1 binding protein, MusTRD1 (muscle TFII-I repeat domain-containing protein 1), which is expressed predominantly in skeletal muscle. Significantly, MusTRD1 contains two repeat domains which show remarkable homology to the six repeat domains of the recently cloned transcription factor TFII-I. Furthermore, both TFII-I and MusTRD1 bind to similar but distinct sequences, which happen to conform with the initiator (Inr) consensus sequence. Given the roles of MEF2 and basic helix-loop-helix (bHLH) proteins in muscle gene expression, the similarity of TFII-I and MusTRD1 is intriguing, as TFII-I is believed to coordinate the interaction of MADS-box proteins, bHLH proteins, and the general transcription machinery.

* Corresponding author. Mailing address: Muscle Development Unit, Children's Medical Research Institute, Locked Bag 23, Wentworthville, New South Wales 2145, Australia. Phone: 61-2-9687-2800. Fax: 61-2-9687-2120. E-mail: ehardeman{at}cmri.usyd.edu.au.

Molecular and Cellular Biology, November 1998, p. 6641-6652, Vol. 18, No. 11
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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