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Originally published In Press as doi:10.1074/jbc.M007002200 on November 13, 2000

J. Biol. Chem., Vol. 276, Issue 4, 2576-2585, January 26, 2001
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Cloning of Human Acetyl-CoA Carboxylase beta  Promoter and Its Regulation by Muscle Regulatory Factors*

Jae-Jung LeeDagger §, Young-Ah MoonDagger , Joo-Hun Ha, Do-Jun Yoon||, Yong-Ho AhnDagger , and Kyung-Sup KimDagger **

From the Dagger  Department of Biochemistry and Molecular Biology, the Institute of Genetic Science, Yonsei University College of Medicine, 134 Shinchon-dong Seodaemun-gu, Seoul, 120-752, Korea, the  Department of Molecular Biology, Kyung-Hee University College of Medicine, Seoul, 130-050, Korea, and the || Department of Biochemistry, Kwandong University College of Medicine, Kangnung, 210-701, Korea

The 280-kDa beta -isoform of acetyl-CoA carboxylase (ACCbeta ) is predominantly expressed in heart and skeletal muscle, whereas the 265-kDa alpha -isoform (ACCalpha ) is the major ACC in lipogenic tissues. The ACCbeta promoter showed myoblast-specific promoter activity and was strongly induced by MyoD in NIH3T3 cells. Serial deletions of the promoter revealed that MyoD acts on the E-boxes located at positions -498 to -403 and on the proximal region including the 5'-untranslated region. Destruction of the E-boxes at positions -498 to -403 by site-directed mutagenesis resulted in a significant decrease of MyoD responsiveness. The "TGAAA" at -32 to -28 and the region around the transcription start site play important roles in basal transcription, probably as a TATA box and an Inr element, respectively. Mutations of another E-box at -14 to -9 and a "GCCTGTCA" sequence at +17 to +24 drastically decreased the MyoD responsiveness. The novel cis-element GCCTGTCA was preferentially bound by MyoD homodimer in EMSA and conferred MyoD responsiveness to a luciferase reporter, which was repressed by the overexpression of E12. This finding is unique since activation via E-boxes is mediated by heterodimers of MyoD and E-proteins. We screened a human skeletal muscle cDNA library to isolate clones expressing proteins that bind to the region around the GCCTGTCA (+8 to +27) sequence, and isolated Myf4 and Myf6 cDNAs. Electrophoretic mobility shift assay showed that recombinant Myf4 and Myf6 bind to this novel cis-element. Moreover, transient expression of Myf6 induced significant activation on the ACCbeta promoter or an artificial promoter harboring this novel cis-element. These findings suggest that muscle regulatory factors, such as MyoD, Myf4, and Myf6, contribute to the muscle-specific expression of ACCbeta via E-boxes and the novel cis-element GCCTGTCA.

* This work was supported in part by Yonsei University College of Medicine for Research Instructors Research Grant 1998-01 and financial support of the Korean Research Foundation for the program year of 1998.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequences of PIbeta and PIIbeta have been submitted to the GenBankTM/EBI Data Bank with accession numbers AF268378 and AF268379, respectively.

§ Recipient of a scholarship from the Brain Korea 21 Project For Medical Science, Ministry of Education, South Korea.

** To whom correspondence and reprint requests should be addressed: Dept. of Biochemistry and Molecular Biology, Institute of Genetic Science, Yonsei University College of Medicine, 134 Shinchon-dong Seodaemun-gu, Seoul 120-752, Korea. Tel.: 82-2-361-5186; Fax: 82-2-312-5041; E-mail: kyungsup59@yumc.yonsei.ac.kr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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