Molecular and General Genetics MGG

, Volume 218, Issue 2, pp 229–239

Structure and expression of the gene encoding the periplasmic arylsulfatase of Chlamydomonas reinhardtii

  • Eugenio L. de Hostos
  • James Schilling
  • Arthur R. Grossman

DOI: 10.1007/BF00331273

Cite this article as:
de Hostos, E.L., Schilling, J. & Grossman, A.R. Molec Gen Genet (1989) 218: 229. doi:10.1007/BF00331273


Chlamydomonas reinhardtii produces a periplasmic arylsulfatase in response to sulfur deprivation. We have isolated and sequenced arylsulfatase cDNAs from a λ gt11 expression library. The amino acid sequence of the protein, as deduced from the nucleotide sequence, has features characteristic of secreted proteins, including a signal sequence and putative glycosylation sites. The gene has a broad codon usage with seven codons, all having A residues in the third position, not previously observed in C. reinhardtii genes. Arylsulfatase transcription is tightly regulated by sulfur availability. The ∼2.7 kb arylsulfatase transcript is very susceptible to degradation, disappearing in less than an hour after sulfur starved cells are administered either sulfate or α-amanitin. The accumulation of the arylsulfatase transcript is also suppressed by the addition of cycloheximide. Transcription initiation from the arylsulfatase gene occurs ∼ 100 bp upstream of the initiation codon, in a region that is 5′ to a 43 bp imperfect inverted repeat. Preceding the transcription start site are sequences similar to those present in promoter regions of other genes from C. reinhardtii.

Key words

Clamydomonas Arylsulfatase λ gt11 Codon usage Sulfate regulation 

Copyright information

© Springer-Verlag 1989

Authors and Affiliations

  • Eugenio L. de Hostos
    • 1
  • James Schilling
    • 2
  • Arthur R. Grossman
    • 3
  1. 1.Department of Biological SciencesStanford UniversityStanfordUSA
  2. 2.California BiotechnologyMountain ViewUSA
  3. 3.Department of Plant BiologyCarnegie Institution of WashingtonStanfordUSA
  4. 4.Abteilung ZellbiologieMax Planck Institut für BiochemieMartinsriedFederal Republic of Germany

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