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J Biol Chem, Vol. 273, Issue 44, 28912-28920, October 30, 1998
Mak21p of Saccharomyces cerevisiae, a Homolog of
Human CAATT-binding Protein, Is Essential for 60 S Ribosomal
Subunit Biogenesis
Herman K.
Edskes,
Yasuyuki
Ohtake, and
Reed B.
Wickner
From the Laboratory of Biochemistry and Genetics, NIDDK, National
Institutes of Health, Bethesda, Maryland 20892-0830
Mak21-1 mutants are unable to
propagate M1 double-stranded RNA, a satellite of the L-A
double-stranded RNA virus, encoding a secreted protein toxin lethal to
yeast strains that do not carry M1. We cloned
MAK21 using its map location and found that Mak21p is
homologous to a human and mouse CAATT-binding protein and open reading
frames in Schizosaccharomyces pombe and
Caenorhabditis elegans. Although the human protein
regulates Hsp70 production, Mak21p is essential for growth and
necessary for 60 S ribosomal subunit biogenesis. mak21-1
mutants have decreased levels of L-A coat protein and L-A
double-stranded RNA. Electroporation with reporter mRNAs shows that
mak21-1 cells cannot optimally express mRNAs which,
like L-A viral mRNA, lack 3'-poly(A) or 5'-cap structures but can
normally express mRNA with both cap and poly(A). The virus propagation phenotype of mak21-1 is suppressed by
ski2 or ski6 mutations, each of which
derepresses translation of non-poly(A) mRNA.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.
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