A phylogeny of cycads (Cycadales) inferred from chloroplast matK gene, trnK intron, and nuclear rDNA ITS region

Mol Phylogenet Evol. 2005 Oct;37(1):214-34. doi: 10.1016/j.ympev.2005.01.006. Epub 2005 Apr 1.


Phylogenetic relationships among the three families and 12 living genera of cycads were reconstructed by distance and parsimony criteria using three markers: the chloroplast matK gene, the chloroplast trnK intron and the nuclear ITS/5.8S rDNA sequence. All datasets indicate that Cycadaceae (including only the genus Cycas) is remotely related to other cycads, in which Dioon was resolved as the basal-most clade, followed by Bowenia and a clade containing the remaining nine genera. Encephalartos and Lepidozamia are closer to each other than to Macrozamia. The African genus Stangeria is embedded within the New World subfamily Zamiodeae. Therefore, Bowenia is an unlikely sister to Stangeria, contrary to the view that they form the Stangeriaceae. The generic status of Dyerocycas and Chigua is unsupportable as they are paraphyletic with Cycas and the Zamia, respectively. Nonsense mutations in the matK gene and indels in the other two datasets lend evidence to reinforce the above conclusions. According to the phylogenies, the past geography of the genera of cycads and the evolution of character states are hypothesized and discussed. Within the suborder Zamiieae, Stangeria, and the tribe Zamieae evolved significantly faster than other genera. The matK gene and ITS/5.8S region contain more useful information than the trnK intron in addressing phylogeny. Redelimitations of Zamiaceae, Stangeriaceae, subfamily Encephalartoideae and subtribe Macrozamiineae are necessary.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chloroplasts / genetics*
  • Cycadopsida / classification*
  • Cycadopsida / genetics*
  • DNA, Plant
  • DNA, Ribosomal / genetics*
  • Evolution, Molecular
  • Geography
  • Introns / genetics
  • NADH Dehydrogenase
  • Phylogeny*


  • DNA, Plant
  • DNA, Ribosomal
  • NADH Dehydrogenase