Supramolecular assemblies of mRNA direct the coordinated synthesis of type I procollagen chain

Arthur Veis, S. J. Leibovich, J. Evans, T. Z. Kirk

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

Registration of the three procollagen α chains and assembly of the triple-helical procollagen molecules takes place in the rough endoplasmic reticulum, but the exact location and timing of assembly is not known. As part of a study of the mechanism of molecular assembly, intact collagen-producing polyribosomes from embryonic chicken tendon fibroblasts have been examined by the techniques of rotary shadowing and electron microscopy. Intact mRNA strands corresponding in length to ~ 4500 bases and complete procollagen α(I) chains have been observed. The mRNA strands are comprised of two mRNA chains. The ribosomes are present in pairs separated along the duplex strand by about 100 nm. The intact polysome is asymmetric; two duplex strands join, and large ribosome aggregates appear. These aggregates are dispersed by collagenase digestion, leaving separate duplex strands with ribosome pairs intact. Ribonuclease digestion yields mixtures of monosomes and ribosome aggregates. Sequential ribonuclease and collagenase digestions yield only monosomes. We propose that each ribosome reads one mRNA chain, so that each pair is thus translating two chains in synchrony. Thus, the complex morphology of the collagen-producing polyribosomes suggests that the organization of a single molecule begins by the organization of the mRNA chains themselves.

Original languageEnglish (US)
Pages (from-to)3693-3697
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume82
Issue number11
DOIs
StatePublished - Jan 1 1985

ASJC Scopus subject areas

  • General

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