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Originally published as Genetics Published Articles Ahead of Print on June 8, 2005.
Genetics, Vol. 171, 393-401, September 2005, Copyright © 2005
doi:10.1534/genetics.105.044644
Mutational Analysis of the pH Signal Transduction Component PalC of Aspergillus nidulans Supports Distant Similarity to BRO1 Domain Family Members
Joan Tilburn*,1,
Juan C. Sánchez-Ferrero
,
Elena Reoyo,
Herbert N. Arst, Jr.* and
Miguel A. Peñalva
* Department of Infectious Diseases, Faculty of Medicine, Imperial College London, London W12 0NN, United Kingdom and Departamento de Microbiología Molecular, Centro de Investigaciones Biológicas CSIC, Madrid 28040, Spain
1 Corresponding author: Department of Infectious Diseases, Imperial College London, Hammersmith Hospital Campus, Ducane Rd., London W12 0NN, United Kingdom.
E-mail: j.tilburn{at}imperial.ac.uk
The alkaline ambient pH signal transduction pathway component PalC has no assigned molecular role. Therefore we attempted a gene-specific mutational analysis and obtained 55 new palC loss-of-function alleles including 24 single residue substitutions. Refined similarity searches reveal conserved PalC regions including one with convincing similarity to the BRO1 domain, denoted PCBROH, where clustering of mutational changes, including PCBROH key residue substitutions, supports its structural and/or functional importance. Since the BRO1 domain occurs in the multivesicular body (MVB) pathway protein Bro1/Vps31 and also the pH signal transduction protein PalA (Rim20), both of which interact with MVB component (ESCRT-III protein) Vps32/Snf7, this might reflect a further link between the pH response and endocytosis.
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