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Molecular evidence of fungal signatures in the marine protist Corallochytrium limacisporum and its implications in the evolution of animals and fungi

DRS at CSIR-National Institute of Oceanography

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Title Molecular evidence of fungal signatures in the marine protist Corallochytrium limacisporum and its implications in the evolution of animals and fungi
 
Creator Manohar, C.S.
Raghukumar, S.
Kasbekar, D.P.
Raghukumar, C.
 
Subject ?-aminoadipate reductase
C. limacisporum
marine protist
sterol C-14 reductase
 
Description Fungi, animals and single-celled organisms belonging to the choanozoans together constitute the supergroup Opisthokonta. The latter are considered crucial in understanding the evolutionary origin of animals and fungi. The choanozoan Corallochytrium limacisporum is an enigmatic marine protist of considerable interest in opisthokontan evolution. Several isolates of the organism were obtained from a coral reef lagoon in the Lakshadweep group of islands of the Arabian Sea. The capability of these cultures to grow on media containing inorganic nitrogen sources prompted us to examine the possible presence of fungal signatures, namely the enzyme ?-aminoadipate reductase (?-AAR) involved in the ?-aminoadipate (AAA) pathway for synthesizing lysine and ergosterol, in one of the isolates. These features, as well as the sterol C-14 reductase gene involved in the sterol pathway of animals and fungi were detected in the organism. Phylogenetic trees based on the ?-AAR gene suggested that Corallochytrium limacisporum is a sister clade to fungi, while those based on the C-14 gene did not adequately resolve whether the organism was more closely related to fungi or animals. While many studies indicate that Corallochytrium is a sister clade to animals, we suggest that further studies are required to examine if the protist is in fact more closely related to fungi rather than animals.
 
Date 2006-07-29T10:44:08Z
2006-07-29T10:44:08Z
2006
 
Type Journal Article
 
Identifier Protist, vol.157(4), 363-376p.
http://drs.nio.org/drs/handle/2264/234
 
Language en
 
Rights An edited version of this paper was published by Elsevier. Copyright [2006] Elsevier
 
Format 865627 bytes
application/pdf
 
Publisher Elsevier