Binding of wheat germ ribosomes to fragmented viral mRNA.

Abstract:

:The specificity of binding of wheat germ ribosomes to mRNA was greatly altered by cleavage of the message. Fragmentation of reovirus mRNA allowed wheat germ ribosomes to bind and protect a variety of internal sequences which were not accessible to ribosomes in the intact message. In experiments using the polycistronic mRNA from bacteriophage R17, wheat germ ribosomes bound preferentially at the beginning of the lysis peptide and synthetase cistrons, and at a third site which may be derived from the C-terminal region of the A protein cistron. This result is similar to that reported previously in a mammalian translational system (J.F. Atkins et al., Cell 18:246-256, 1979) except that, in the present study, limited cleavage of the phage RNA was necessary to activate these sites. More extensive fragmentation of R17 RNA permitted wheat germ ribosomes to bind and protect a great many additional sites. Thus, presence of an (exposed) 5'-terminus on an RNA molecule appears to be necessary and sufficient for attachment of eucaryotic ribosomes.

journal_name

J Virol

journal_title

Journal of virology

authors

Kozak M

doi

10.1128/JVI.35.3.748-756.1980

subject

Has Abstract

pub_date

1980-09-01 00:00:00

pages

748-56

issue

3

eissn

0022-538X

issn

1098-5514

journal_volume

35

pub_type

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