Isolation and characterization of initiation fragments from lens 10S and 14S alpha-crystallin messenger ribonucleic acids.
The alpha-crystallin 10S and 14S messenger ribonucleic acids (mRNAs) for the B and A chains, respectively, were isolated from calf lenses. Initiation complexes were formed with both mRNAs after which the unprotected regions were digested with ribonuclease T1. A single fragment of approximately 45 nucleotides was obtained from both the 10S and 14S mRNAs. The fragments retained the ability to reform initiation complexes under standard conditions. Two-dimensional fractionation of ribonuclease T1 digests indicated considerable similarity between the 10S and 14S fragments. However, marked differences in the (U)G region were observed. The addition of the methylating agent S-adenosyl-L-methionine to the mRNA initiation system increases complex formation form two to five times, suggesting that methylation may be required for initiation.
D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000378:metabolism; D002417:Cattle; D003459:Crystallins / Q000096:biosynthesis*; D007908:Lens, Crystalline / Q000378:metabolism*; D008970:Molecular Weight; D010944:Plants / Q000378:metabolism; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism; D014908:Triticum / Q000378:metabolism
D003459:Crystallins; D012333:RNA, Messenger