Molecular and Cellular Biochemistry

, Volume 63, Issue 2, pp 131–136 | Cite as

Structural organization of high-Mr mammalian aminoacyl-tRNA synthetases

Comparison of multi-enzyme complexes from different sources
  • Chi V. Danga
  • Chuan V. Dang
Original Articles
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  • 30 Downloads

Summary

Many mammalian aminoacyl-tRNA synthetases have been isolated as high-Mr multi-enzyme complexes. These complexes often contain variable contents of synthetase activities. The complexes may also contain molecules other than synthetases such as tRNA. The observed variations in size, polypeptide composition, and content of enzyme activities of the high-Mr synthetase complexes have been sources of confusion in the understanding of the structural organization of these complexes. A unified scheme of structural organization which encompasses most observations on high-Mr complexes reported in the literature is presented.

Keywords

aminoacyl-tRNA synthetase multi-enzyme complex protein biosynthesis 
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Copyright information

© Martinus Nijhoff Publishers 1984

Authors and Affiliations

  • Chi V. Danga
    • 1
  • Chuan V. Dang
    • 2
  1. 1.Department of MedicineJohns Hopkins University, School of MedicineBaltimoreUSA
  2. 2.Department of Biochemistry, School of MedicineLoma Linda UniversityLoma LindaUSA

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