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J. Biol. Chem., Vol. 277, Issue 41, 38781-38790, October 11, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/41/38781    most recent M201559200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kim, M. Articles by Pai, H.-S. Search for Related Content PubMed PubMed Citation Articles by Kim, M. Articles by Pai, H.-S. Social Bookmarking                      What's this?

Forkhead-associated Domains of the Tobacco NtFHA1 Transcription Activator and the Yeast Fhl1 Forkhead Transcription Factor Are Functionally Conserved^*

Moonil Kim^§, Joon-Woo Ahn, Kiwon Song^¶, Kyung-Hee Paek^§, and Hyun-Sook Pai

From the  Laboratory of Plant Genomics, Korea Research Institute of Bioscience and Biotechnology, Yusong, Taejon 305-333, the ^¶ Department of Biochemistry, Yonsei University, Seoul 120-749, and the ^§ Graduate School of Biotechnology, Korea University, Seoul 136-701, Korea

NtFHA1 encodes a novel protein containing the forkhead-associated (FHA) domain and the acidic domain in Nicotiana tabacum. NtFHA1 functions as a transactivator and is targeted to the nucleus. The sequence of the FHA domain of NtFHA1 is significantly homologous to that of the Fhl1 forkhead transcription factor of yeast. FHL1 was previously identified as a suppressor of RNA polymerase III mutations, and the fhl1 deletion mutant exhibited severe growth defects and impaired rRNA processing. Ectopic expression of the FHA domain of NtFHA1 (but not its mutant form) resulted in severe growth retardation in yeast. Similarly, expression of Fhl1, its FHA domain, or chimeric Fhl1 containing the NtFHA1 FHA domain also inhibited yeast growth. Yeast cells overexpressing the FHA domains of NtFHA1 and Fhl1 contained lower levels of mature rRNAs and exhibited rRNA-processing defects, similar to the fhl1 null mutant. Chimeric Fhl1 (but not the mutant form with a small deletion in its FHA domain) fully complemented the growth and rRNA-processing defects of the fhl1 null mutant, demonstrating that the FHA domain of NtFHA1 can functionally substitute for the FHA domain of Fhl1. These results demonstrate that the FHA domains of NtFHA1 and Fhl1 are conserved in their structure and function and that the FHA domain of Fhl1 is critically involved in regulation of rRNA processing in yeast. NtFHA1 function in plants may be analogous to Fhl1 function in yeast.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AF411856.

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				E. R. Morris, D. Chevalier, and J. C. Walker DAWDLE, a Forkhead-Associated Domain Gene, Regulates Multiple Aspects of Plant Development Plant Physiology, July 1, 2006; 141(3): 932 - 941. [Abstract] [Full Text] [PDF]