Predicted glycosyltransferases promote development and prevent spurious cell clumping in the choanoflagellate S. rosetta

Elife. 2018 Dec 17:7:e41482. doi: 10.7554/eLife.41482.

Abstract

In a previous study we established forward genetics in the choanoflagellate Salpingoeca rosetta and found that a C-type lectin gene is required for rosette development (Levin et al., 2014). Here we report on critical improvements to genetic screens in S. rosetta while also investigating the genetic basis for rosette defect mutants in which single cells fail to develop into orderly rosettes and instead aggregate promiscuously into amorphous clumps of cells. Two of the mutants, Jumble and Couscous, mapped to lesions in genes encoding two different predicted glycosyltransferases and displayed aberrant glycosylation patterns in the basal extracellular matrix (ECM). In animals, glycosyltransferases sculpt the polysaccharide-rich ECM, regulate integrin and cadherin activity, and, when disrupted, contribute to tumorigenesis. The finding that predicted glycosyltransferases promote proper rosette development and prevent cell aggregation in S. rosetta suggests a pre-metazoan role for glycosyltransferases in regulating development and preventing abnormal tumor-like multicellularity.

Keywords: S. rosetta; evolutionary biology; genetic screen; genetics; genomics; glycosyltransferase; multicellularity.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Adhesion / genetics
  • Choanoflagellata / cytology
  • Choanoflagellata / genetics*
  • Choanoflagellata / metabolism
  • Extracellular Matrix / metabolism
  • Extracellular Matrix Proteins / metabolism
  • Glycosylation
  • Glycosyltransferases / genetics*
  • Glycosyltransferases / metabolism
  • Mutation*
  • Phenotype
  • Protozoan Proteins / genetics*
  • Protozoan Proteins / metabolism
  • Receptors, Cell Surface / metabolism
  • Sequence Homology, Amino Acid

Substances

  • Extracellular Matrix Proteins
  • Protozoan Proteins
  • Receptors, Cell Surface
  • extracellular matrix receptor
  • Glycosyltransferases