Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2004 Aug;41(8):805-12.
doi: 10.1016/j.fgb.2004.04.003.

The eln3 gene involved in fruiting body morphogenesis of Coprinus cinereus encodes a putative membrane protein with a general glycosyltransferase domain

Affiliations

The eln3 gene involved in fruiting body morphogenesis of Coprinus cinereus encodes a putative membrane protein with a general glycosyltransferase domain

Toshihide Arima et al. Fungal Genet Biol. 2004 Aug.

Abstract

We identified and characterized elongationless3 (eln3-1), a restriction enzyme-mediated integration (REMI) mutation affecting fruiting body morphogenesis in Coprinus cinereus. The mutant produces an aberrant fruiting body in which the stipe hardly elongates during fruiting body maturation. In the wild type, cylindrical stipe cells, elongation growth of which is responsible for stipe elongation, make side-by-side contact with one another and run parallel to the stipe axis, whereas in the mutant, the organization of the stipe tissue is disturbed and much space is produced between stipe cells. This disorganization of the stipe tissue, together with reduced elongation of the stipe cells, causes the mutant stipe short and bulgy. After a plasmid rescue, the eln3 gene was identified as a DNA fragment that complements the eln3-1 mutation. The eln3 ORF is predicted to encode a protein of 927 amino acids with a general glycosyltransferase domain and to be located in the plasma membrane. Transcription of the eln3 gene is specifically activated in rapidly elongating stipes. Possible involvement of the putative Eln3 enzyme in cell-to-cell connection is discussed.

PubMed Disclaimer

Similar articles

Cited by

Publication types

MeSH terms

LinkOut - more resources