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Gene Review

FHL1  -  Fhl1p

Saccharomyces cerevisiae S288c

Synonyms: P8283.15, Pre-rRNA-processing protein FHL1, YPR104C
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High impact information on FHL1

  • We show that regulation of RP gene transcription via TOR and PKA in yeast involves the Forkhead-like transcription factor FHL1 and the two cofactors IFH1 (a coactivator) and CRF1 (a corepressor) [1].
  • TOR regulates ribosomal protein gene expression via PKA and the Forkhead transcription factor FHL1 [1].
  • In turn, Sfp1 influences the nuclear localization of Fhl1 and Ifh1, which bind to RP gene promoters [2].
  • Loss of functional Fhl1p leads to cells that have only 20% the normal amount of RNA and that synthesize ribosomes at only 5-10% the normal rate [3].
  • In vitro transcription of a UAS(RAP1) enhancer-driven reporter gene requires both Rap1p and TFIID and is independent of the Fhl1p-Ifh1p coregulator [4].

Biological context of FHL1

  • Conversely, its overexpression by increased gene dosage partially compensates for the genetic inactivation of Fhl1p [5].
  • Carboxy-terminal deletions removing the last third of the protein lead to a leaky growth phenotype with impaired rRNA maturation, as in the case of the fhl1 deletion [5].
  • IFH1 (located on chromosome IV) was isolated as a dosage-dependent suppressor partially correcting the growth defect of the fhl1 deletion [5].
  • One of these upstream activation sequence elements has an ATGTACGGATGT motif, which has previously been described as a putative binding site for the forkhead-like transcription factor Fhl1p [6].
  • Two other genes, FHL1 and PEP5, are involved in the control of ribosome formation and vacuole biogenesis, respectively; and five genes, presently having unknown functions, could be new potentially interesting candidates for further studies in relation to yeast replicative aging [7].

Associations of FHL1 with chemical compounds

  • Deletion of FHL1 reduces CPC2 transcription significantly in presence of glucose, but has no effect when the non-fermentable carbon source ethanol is provided [6].
  • Increased amounts of the Fhl1p co-regulator Ifh1p induce CPC2 transcription even when ethanol is utilized [6].

Physical interactions of FHL1

  • Surprisingly, loss of Hmo1 abolishes binding of Fhl1 and Ifh1 to RP promoters but does not significantly affect the level of transcriptional activity [8].

Other interactions of FHL1

  • Hmo1 binding to RP promoters requires Rap1 and (to a lesser extent) Fhl1, proteins that also associate with RP promoters [8].
  • Occasionally, multiseptate cells were also produced, indicating the involvement of fhl1 and fkh2 in efficient septum cleavage [9].


  1. TOR regulates ribosomal protein gene expression via PKA and the Forkhead transcription factor FHL1. Martin, D.E., Soulard, A., Hall, M.N. Cell (2004) [Pubmed]
  2. A dynamic transcriptional network communicates growth potential to ribosome synthesis and critical cell size. Jorgensen, P., Rupes, I., Sharom, J.R., Schneper, L., Broach, J.R., Tyers, M. Genes Dev. (2004) [Pubmed]
  3. Central role of Ifh1p-Fhl1p interaction in the synthesis of yeast ribosomal proteins. Rudra, D., Zhao, Y., Warner, J.R. EMBO J. (2005) [Pubmed]
  4. Yeast TFIID serves as a coactivator for Rap1p by direct protein-protein interaction. Garbett, K.A., Tripathi, M.K., Cencki, B., Layer, J.H., Weil, P.A. Mol. Cell. Biol. (2007) [Pubmed]
  5. The IFH1 gene product interacts with a fork head protein in Saccharomyces cerevisiae. Cherel, I., Thuriaux, P. Yeast (1995) [Pubmed]
  6. The yeast CPC2/ASC1 gene is regulated by the transcription factors Fhl1p and Ifh1p. Kleinschmidt, M., Schulz, R., Braus, G.H. Curr. Genet. (2006) [Pubmed]
  7. Sir-dependent downregulation of various aging processes. Daniel, J. Mol. Genet. Genomics (2005) [Pubmed]
  8. An HMG protein, Hmo1, associates with promoters of many ribosomal protein genes and throughout the rRNA gene locus in Saccharomyces cerevisiae. Hall, D.B., Wade, J.T., Struhl, K. Mol. Cell. Biol. (2006) [Pubmed]
  9. Characterisation of two novel fork-head gene homologues of Schizosaccharomyces pombe: their involvement in cell cycle and sexual differentiation. Szilagyi, Z., Batta, G., Enczi, K., Sipiczki, M. Gene (2005) [Pubmed]
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