The Secondary Structure and Poly(A) Content of Globin Messenger RNA as a Pure RNA and in Polyribosome-Derived Ribonucleoprotein Complexes

Favre, Alain; Morel, Carlos Médicis; Scherrer, Klaus

doi:10.1111/j.1432-1033.1975.tb02285.x

Cited by 59 publications

(21 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Regions of secondary structure have been observed in various mRNA's (46), including the 14S lens mRNA (40). If the excess nucleotides really represent secondary structures that are not involved in coding, they have been extremely conservative in evolution, at least as far as their dimension is concerned.…”

Section: The A-crystaliin Messengersmentioning

confidence: 99%

The Vertebrate Eye Lens

Bloemendal

1977

Science

444

147

View full text Add to dashboard Cite

Section: The A-crystaliin Messengersmentioning

confidence: 99%

The Vertebrate Eye Lens

Bloemendal

1977

Science

444

147

View full text Add to dashboard Cite

“…Electron microscopy data obtained by dark-field visualization of duck globin 15 S mRNP particles has shown that proteins are distributed al ong all of the messenger molecule although not uniformly (8). Data obtained using optical methods have shown the highly bi-helical conformation of duck-globin mRNA and a strong interaction of proteins with mRNA and its poly(A) sequence at the 3'-OH end (9,10).…”

Section: Introductionmentioning

confidence: 99%

Evidence for the protection of specific RNA sequences in globin messenger ribonucleoprotein particles

Goldenberg¹,

Víncent²,

Scherrer³

1979

Nucl Acids Res

Self Cite

View full text Add to dashboard Cite

Purified 15 S globin mRNA-protein (mRNP) complexes obtained by EDTA dissociation of duck reticulocytes polyribosomes were digested with the calcium dependant Staphytococcus auLeuz nuclease (EC 3. 1. 4. 7.). 25 % of the globin mRNA sequences were resistant to extensive nuclease digestion as determined by TCA precipitation of the digested 15 S particles labelled in vivo with tritiated uridine.Polyacrylamide gel electrophoresis of the RNA from nuclease digested 15 S particles showed that the protected oligoribonucleotides were distributed into two distinct size classes of 25,000 and 12,000 MW. Comparison between in wvtAo iodine-labelled 9 S globin mRNA and RNA extracted from Staphylococcal nuclease digested 15 S mRNP particles was carried out by fingerprinting. Mapping of T1 ribonuclease digests by high-voltage electrophoresis and homochromatography showed that specific oligoribonucleotides were protected against nuclease attack by proteins of the 15 $ mRNP. INTRODUCTIONMessenger RNA in the reticulocyte cytoplasm is associated with proteins to form messenger ribonucleoprotein (mRNP) complexes. In the case of globin m RNA 2 kinds of mRNP complexes have been previously described: the actively

show abstract

“…Physical studies reveal that globin mRNAs (48,49), like RNA phages (4, 50), have considerable secondary structure. According to a plausible secondarx structure model of phage MS2 RNA (4), doublestranded regions diverge at a rate 2.5-fold lower than singlestranded regions (26).…”

Section: G C C C C U U G a G C A U C U G A C U U C U G G C U A A U A mentioning

confidence: 99%

Molecular evolution of human and rabbit beta-globin mRNAs.

Kafatos¹,

Efstratiadis²,

Forget³

et al. 1977

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

148

View full text Add to dashboard Cite

The primary structures of human and rabbit fl-globin mRNAs are compared. Using as a standard the extent of nucleotide substitutions inferred from the hypervariable amino acid residues of fibrinopeptides A and B, which are thought to change largely by neutral evolution, we show that not all silent mutations in globin mRNA are neutral. The divergence of the sequences is limited in part by the selective usage of synonymous codons. The divergent nucleotides tend to be distributed nonrandomly: in the coding region silent substitutions are most rare in segments that are also deficient in substitutions leading to replacements.Until recently, the molecular evolution of nucleic acids could not be studied with the directness possible for proteins (1), because the information was based largely on reassociation and hybridization data, or on inferences from protein sequences. However, simplified DNA (2, 3) and RNA sequencing techniques are now available, and should provide a rapid increase in our direct knowledge of the primary structure of genes. (11,12) and divided by the time elapsed since divergence of the two species. However, if two pairs of sequences (e.g., /-globin mRNAs and fibrinopeptide mRNAs; see below) are being compared in the same two species, or in species that have diverged at the same time, the percent substitution values can be treated directly as nonlinear substitution rates. This is very useful, because paleontological estimates of the time of divergence are often subject to considerable uncertainty (13,14).Replacement-corrected percent substitution. By definition, in some silent substitution sites some substitutions may lead to amino acid replacement (e.g., U -G in CAU). To correct for possible substitutions leading to replacements, the number of silent sites can be multiplied by a "replacement correction" factor, which is the sum of possible substitutions that would be silent, divided by the sum of all possible substitutions (i.e., 3 times the number of sites).A neutrality standard for mRNA sequences The "neutral mutation-random drift" theory (15-17) implies that some features of macromolecules are relatively unimportant, so that a significant number of neutral mutations are possible and can be fixed in the population by random drift.Neutralists agree that many mutants are deleterious and therefore nonobserved. However, sometimes they consider all or nearly all possible silent mutations as neutral (18,12), which would imply that no appreciable selection is operating on the mRNA itself (e.g., on processing, secondary structure, stability, translatability, etc.

show abstract

The Secondary Structure and Poly(A) Content of Globin Messenger RNA as a Pure RNA and in Polyribosome-Derived Ribonucleoprotein Complexes

Cited by 59 publications

References 40 publications

The Vertebrate Eye Lens

The Vertebrate Eye Lens

Evidence for the protection of specific RNA sequences in globin messenger ribonucleoprotein particles

Molecular evolution of human and rabbit beta-globin mRNAs.

Contact Info

Product

Resources

About