Polyadenylic Acid Sequences in the Virion RNA of Poliovirus and Eastern Equine Encephalitis Virus

Armstrong, John A.; Edmonds, Mary; Nakazato, Hiroshi; Phillips, Bruce A.; Vaughan, Maurice H.

doi:10.1126/science.176.4034.526

Cited by 148 publications

(46 citation statements)

References 22 publications

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“…Mitochondrial poly(A) is not involved in a similar type of transport, since the mitochondrial messenger-like RNA is both synthesized and used within the mitochondria (S. Perlman, unpublished observation). The size of mitochondrial poly(A) is the same as that of poliovirus (30,31). Poliovirus RNA, like mitochondrial RNA, is not transported to polyribosomes from its site of synthesis.…”

Section: Resultsmentioning

confidence: 59%

Mitochondrial Protein Synthesis: RNA with the Properties of Eukaryotic Messenger RNA

Perlman

Abelson

Penman

1973

Proc. Natl. Acad. Sci. U.S.A.

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A heterogeneous RNA fraction with properties resembling those of messenger RNA was identified in mammalian mitochondria. Synthesis of contaminating RNA of nuclear origin was suppressed by treatment with camptothecin. Labeling of the messenger-like RNA is completely inhibited by ethidium bromide, a specific inhibitor of mitochondrial functions.Although mitochondrial protein synthesis resembles that of prokaryotes in several regards, the messenger-like RNA is covalently linked to poly(adenylic acid) [poly(A)J. Poly(A) has thus far been found only in eukaryotic cells. The poly(A) segment has a gel electrophoretic mobility of about 4 S, corresponding to a length of 50-80 nucleotides, and thus resembles in size the poly(A) found in some mammalian viral RNAs. The messenger RNA can be released from the mitochondrial protein-synthesizing structure by treatment with puromycin.Mitochondria of eukaryotic cells have a distinct system of protein synthesis that is quite dissimilar from that found in the cellular cytoplasm. The ribosome-like structure of mitochondria is relatively small (60 S) (1-4). Mitochondrial protein synthesis is sensitive to chloramphenicol, an inhibitor of prokaryotic ribosomal function, and insensitive to cycloheximide, an inhibitor of eukaryotic protein synthesis. NFormyl-methionine has been found in mitochondria and is presumed to initiate polypeptide synthesis as in bacteria (5, 6).These properties of mitochondrial protein synthesis suggested a similarity to prokaryotic rather than eukaryotic mechanisms, and there has been speculation about a possible origin of mitochondria in a primordial prokaryotic symbiont.In this report, we describe an RNA species synthesized in mitochondria with properties that suggest it serves as messenger RNA for mitochondrial protein synthesis. Surprisingly, this RNA contains polyadenylate segments, which have, so far, been found only in the messenger RNA of eukaryotic cells (7)(8)(9)(10)(11) Analysis of Total Mitochondrial RNA. Cellular extracts were prepared and analyzed as described (13). Briefly, cells were washed and then suspended in 1 ml of RSB buffer [10 mM NaCl-1.5 mM MgCl2-10 mM Tris* HCO (pH 7.4)] before they were broken in a Dounce homogenizer. Nuclei were removed by centrifugation at 800 X g for 2 min. The supernatant was again centrifuged at 7700 X g for 8 min. This pellet (mitochondrial fraction) was resuspended in sodium dodecyl sulfate (SDS) buffer and extracted by the hot phenol-SDS method (14). The RNA was analyzed by electrophoresis on 2.7% acrylamide gels for 3.5 hr at 7.5 V/cm. Gels were fractionated as described (15).Analysis of Poly(A)-Containing RNA. Mitochondrial RNA was labeled in the presence of camptothecin, and a crude mitochondrial fraction was prepared. Mitochondria were suspended in MSB buffer [100 mM NaCl-10 mM MgCl2-10 mM Tris*HCl (pH 7.4)] and lysed with 0.5% sodium deoxycholate-0.5% Brij 58. (Brij 58 was obtained from the Hercules Powder, Co.) The lysed mitochondria were layered on a 15-30% MBS-sucrose gradients and centrifuged ...

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Section: Resultsmentioning

confidence: 59%

Mitochondrial Protein Synthesis: RNA with the Properties of Eukaryotic Messenger RNA

Perlman

Abelson

Penman

1973

Proc. Natl. Acad. Sci. U.S.A.

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“…Although polyadenylation and splicing are linked, they can occur independently (72), and polyadenylation is not an absolute prerequisite for transport, because some nonadenylated RNAs are transported efficiently (3,26,73). Some viral mRNAs are synthesized exclusively in the cytoplasm and are polyadenylated, indicating an extranuclear role for poly(A) (1,5,19). There is evidence for a link between poly(A) and translation, especially in lower organisms (16-18, 21, 47, 62), and some experiments suggest that poly(A) affects mRNA half-lives (see below).…”

mentioning

confidence: 99%

The poly(A)-poly(A)-binding protein complex is a major determinant of mRNA stability in vitro.

Bernstein¹,

Peltz²,

Ross³

1989

Mol. Cell. Biol.

362

186

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“…Four-fold increase of 3H/32p ratio was found for RNAase-resistant fragments in comparison to total mitochondrial [3H,32p] RNA. Thus Millipore-retained RNA and especially RNAaseresistant acid-insoluble material are markedly enriched in adenylic acid content (see [ 16] ).…”

Section: Resultsmentioning

confidence: 99%

Poly(A)‐containing ribonucleic acid in mitochondria from rat liver and Krebs II ascitic carcinoma cells

1973

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Polyadenylic Acid Sequences in the Virion RNA of Poliovirus and Eastern Equine Encephalitis Virus

Cited by 148 publications

References 22 publications

Mitochondrial Protein Synthesis: RNA with the Properties of Eukaryotic Messenger RNA

Mitochondrial Protein Synthesis: RNA with the Properties of Eukaryotic Messenger RNA

The poly(A)-poly(A)-binding protein complex is a major determinant of mRNA stability in vitro.

Poly(A)‐containing ribonucleic acid in mitochondria from rat liver and Krebs II ascitic carcinoma cells

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