The protein moieties of animal messenger ribonucleoproteins

Williamson, Robert

doi:10.1016/0014-5793(73)80413-2

Cited by 66 publications

(20 citation statements)

References 49 publications

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“…Some of these studies indicate that the protein components of the two classes of m R N P , as judged by sodium dodecyl sulfate (NaDodS0,)-polyacrylamide gel electrophoresis, are identical or essentially similar (Baglioni, 1974; Barrieux et al, 1975;van Venrooij et al, 1977), while according to other reports their protein patterns are different (Gander et al, 1973: Liautard et al, 1976). Furthermore, low molecular weight proteins in the 15 000-30 000-dalton range, which resemble the typical ribosomal and/or cellular proteins in size, have been found in variable amounts and numbers in mRNP particles in many of these reports (Gander et al, 1973; Liautard et al, 1976; for a review see Williamson, 1973; Greenberg, 1975).…”

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confidence: 97%

“…Although the reported variations in the size and number of the protein components of eukaryotic polysomal mRNP particles remain a matter of considerable dispute (Williamson, 1973;Greenberg, 1975), the widespread occurrence of the two major proteins of molecular weights 52 000 and 78 000 strongly suggests that they may be specifically associated with nucleotide sequences which are common to most mRNA molecules. With regard to the interrelationship of the protein moieties of free and polysomal m R N P particles, the few published reports in the literature have led to highly conflicting conclusions.…”

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confidence: 99%

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Poly(riboadenylate)-containing messenger ribonucleoprotein particles of chick embryonic muscles

Jain¹,

Sarkar²

1979

Biochemistry

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Poly(A)-containing cytoplasmic messenger ribonucleoprotein (mRNP) particles were isolated from subcellular fractions of 12-1 4-day-old chick embryonic muscles by chromatography on oligo(dT)-cellulose and elution of the bound m R N P with 50% formamide. Two types of mRNP, free or nonpolysomal and polysome-derived, were obtained from the postpolysomal supernatant fraction and EDTAdissociated polysomes, respectively. The m R N P were characterized by the absence of ribosomal RNAs and typical ribosomal proteins, by the presence of a limited number of characteristic proteins, and by the polydisperse sedimentation of the particles and their R N A moieties in sucrose gradients. Although the two types of particles show many similarities, their buoyant densities and NaDodS0,-gel electrophoretograms of their protein moieties indicate that they represent two distinct types of macromolecular complexes. The free m R N P are relatively protein rich and contain 10 distinct proteins in the 40 000-100 000 molecular weight range. The polysome-derived m R N P are comparatively protein deficient I n eukaryotic cells mRNAs are complexed with proteins to form messenger ribonucleoprotein (mRNP)' particles (Perry Greenberg, 1975). Two types of m R N P particles, polysome-derived mRNP, which are released by the dissociation of polyribosomes, and nonpolysomal free mRNP (also referred to as informosomes), have been reported in the literature. The polysomal m R N P particles derived from a large number of species and tissues contain two major proteins of about 52 000 and 78 000 molecular weight and a large number of additional

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confidence: 97%

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Poly(riboadenylate)-containing messenger ribonucleoprotein particles of chick embryonic muscles

Jain¹,

Sarkar²

1979

Biochemistry

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“…Although a number of functions for these proteins in messenger storage, transport, protection, or initiation have been suggested, their precise role in eukaryotic regulation has remained unclear (for general reviews, see refs. [22][23][24].…”

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Interaction of poly(A) and mRNA with eukaryotic initiator met-tRNA-f binding factor: identification of this activity on reticulocyte ribonucleic acid protein particles.

Hellerman¹,

Shafritz²

1975

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

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“…Several classes of specific proteins associated with mRNA have been distinguished [2]. We developed a method for the isolation of a set of proteins with a high affinity for dRNA, extracted from free cytoplasmic dRNP particles [3 1 .…”

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confidence: 99%