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The Plasmodium lophurae (Avian Malaria) Ribosome *
Author(s) -
SHERMAN IRWIN W.,
JONES LYNN A.
Publication year - 1977
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1977.tb00989.x
Subject(s) - ribosome , ribosomal rna , biology , rna , centrifugation , plasmodium (life cycle) , ultracentrifuge , microbiology and biotechnology , biochemistry , virology , parasite hosting , world wide web , gene , computer science
SYNOPSIS. Ribosomes were isolated from Plasmodium lophurae by Triton X‐100 lysis and ultracentrifugation. Plasmodium lophurae ribosomal subparticles, produced by treatment of ribosomes with puromycin, were separated by sucrose gradient centrifugation. The nucleotide base composition of P. lophurae ribosomal RNA (rRNA) from intact ribosomes and subparticles was low in guanine‐cytosine content (∼ 37% G + C) whereas the rRNA of the host cell (duck reticulocyte) was considerably higher (64% G + C). The rRNA of the malaria parasite was typically protozoan, with sedimentation values of 25S and 17S. In vitro , free parasites and malaria‐infected red cells incorporated radioactive adenosine into both the large and the small plasmodial subparticles; label was also recovered in the 25S and 17S RNAs. These results suggest that host ribosomes do not contribute to ribosome biogenesis in this malaria, rather parasite rRNA is the transcription product of plasmodial cistrons.