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

Mol Gen Genet. 1989 Aug;218(2):229-39. doi: 10.1007/BF00331273.

Abstract

Chlamydomonas reinhardtii produces a periplasmic arylsulfatase in response to sulfur deprivation. We have isolated and sequenced arylsulfatase cDNAs from a lambda 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 approximately 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 alpha-amanitin. The accumulation of the arylsulfatase transcript is also suppressed by the addition of cycloheximide. Transcription initiation from the arylsulfatase gene occurs approximately 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.

MeSH terms

  • Amino Acid Sequence
  • Arylsulfatases / biosynthesis
  • Arylsulfatases / genetics*
  • Base Sequence
  • Blotting, Southern
  • Chlamydomonas / genetics*
  • Chromatography, Affinity
  • Cloning, Molecular
  • Codon
  • DNA / genetics
  • DNA / isolation & purification
  • Endonucleases
  • Gene Expression Regulation
  • Genes*
  • Immunochemistry
  • Molecular Sequence Data
  • Nucleic Acid Hybridization
  • RNA / genetics
  • Single-Strand Specific DNA and RNA Endonucleases
  • Sulfatases / genetics*
  • Transcription, Genetic

Substances

  • Codon
  • RNA
  • DNA
  • Endonucleases
  • Single-Strand Specific DNA and RNA Endonucleases
  • Sulfatases
  • Arylsulfatases