Abstract
Ribosomal salt washes of Artemia salina embryos contain a protein(s) that binds [3H]m7GpppGpC and [3H]m7GpppGmpC, as measured by retention on nitrocellulose membrane filters. These oligonucleotides correspond in structure to the methylated 5'-terminal sequences (caps) present in many eukaryotic mRNAs. The cap binding protein does not bind the unmethylated counterparts of caps, e.g., [32P]GpppGpCp, or a derivative of m7GpppGmpC containing ring-opened m7G. None of the purified initiation factors IF-MP, IF-M2A, IF-M2B, IF-M3, or IF-MI binds the m7G-containing oligonucleotides.
MeSH Terms
Base Sequence
Binding, Competitive
Decapoda
Guanine Nucleotides/metabolism,pharmacology
Magnesium/pharmacology
Methylation
Peptide Chain Initiation, Translational/drug effects
Peptide Initiation Factors
Protein Binding/drug effects
Protein Biosynthesis/drug effects
Proteins/metabolism
RNA, Messenger/metabolism
Structure-Activity Relationship
Chemicals
Guanine Nucleotides
Peptide Initiation Factors
Proteins
RNA, Messenger
Magnesium
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Filipowicz W
Furuichi Y
Sierra J M
Muthukrishnan S
Shatkin A J
Ochoa S
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