In:
European Journal of Biochemistry, Wiley, Vol. 38, No. 3 ( 1973-10), p. 443-452
Abstract:
Two RNA · protein complexes were isolated from duck erythroblast postribosomal supernatants. Their nominal sedimentation values on sucrose gradients are 12 S and 20 S, respectively. The 12‐S particle contains a 4–6 S RNA, in the 20‐S particle a 9‐S RNA is found. This 9‐S RNA is shown to direct the synthesis of all duck globin chains in a cell‐free, messenger RNA‐dependent protein‐synthesizing system. The protein moiety of these ribosome‐free particles is described and compared with the proteins found in the mRNA · protein complex liberated by EDTA from polyribosomes. We show that in the free‐cytoplasmic particles no protein can be found which is identical to any of the polypeptides associated with polyribosomal mRNA. Some of these protein are phosphorylated and contain phosphoserine. The electrophoretic patterns of phosphorylated proteins from the two globin mRNA‐containing complexes differ, as do those of the unlabelled polypeptides. We conclude that the mRNA‐associated protein population is exchanged when the mRNA enters the translation machinery. The possible role of the RNA‐associated proteins in the post‐transcriptional and translational control of eukaryotic protein synthesis is discussed.
Type of Medium:
Online Resource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1973.38.issue-3
DOI:
10.1111/j.1432-1033.1973.tb03078.x
Language:
English
Publisher:
Wiley
Publication Date:
1973
detail.hit.zdb_id:
1398347-7
detail.hit.zdb_id:
2172518-4
SSG:
12
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