Translation in vivo and in vitro of mRNAs coding for vitellogenin, serum albumin and very-low-density lipoprotein II from chicken liver. A difference in translational efficiency.

Characterisation of polysomes from estrogenized chicken liver revealed that very-low-density lipoprotein II (VLDLII), serum albumin and vitellogenin mRNAs are differently packed with ribosomes during translation in vivo. Tne ribosome density per number of nucleotides is high for VLDLII mRNA, intermediate for serum albumin mRNA and low for vitellogenin mRNA. This difference in ribosomal load is maintained throughout the period of hormone effect. The differential utilisation observed for vitellogenin and VLDLII mRNAs partly explains the large difference in molar production rate between these yolk protein precursors. Translation properties and efficiency of the three hepatic mRNAs were also compared in the mRNA-depleted reticulocyte lysate. Elongation of the nascent chains for vitellogenin and serum albumin proceeded in a discontinuous fashion. Initiation in vitro was studied at varying ionic strengths, in the presence of aurintricarboxylic acid, and at suboptimal hemin concentrations. VLDLII mRNA expression is by far the most resistant to 7-methylguanosine 5'-triphosphate (m7GTP) and high salt concentrations, vitellogenin mRNA the least. This behaviour resembles the differential utilisation of the mRNAs in vivo. The putative structural basis of these differences is discussed.