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Journal Article

Interplay between trigger factor and other protein biogenesis factors on the ribosome.

MPS-Authors
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Bornemann,  T.
Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Holtkamp,  W.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Wintermeyer,  W.
Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)

2039358.pdf
(Publisher version), 782KB

Supplementary Material (public)

2039358_Suppl.pdf
(Supplementary material), 557KB

Citation

Bornemann, T., Holtkamp, W., & Wintermeyer, W. (2014). Interplay between trigger factor and other protein biogenesis factors on the ribosome. Nature Communications, 5: 4180. doi:10.1038/ncomms5180.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-DBEF-6
Abstract
Nascent proteins emerging from translating ribosomes in bacteria are screened by a number of ribosome-associated protein biogenesis factors, among them the chaperone trigger factor (TF), the signal recognition particle (SRP) that targets ribosomes synthesizing membrane proteins to the membrane and the modifying enzymes, peptide deformylase (PDF) and methionine aminopeptidase (MAP). Here, we examine the interplay between these factors both kinetically and at equilibrium. TF rapidly scans the ribosomes until it is stabilized on ribosomes presenting TF-specific nascent chains. SRP binding to those complexes is strongly impaired. Thus, TF in effect prevents SRP binding to the majority of ribosomes, except those presenting SRP-specific signal sequences, explaining how the small amount of SRP in the cell can be effective in membrane targeting. PDF and MAP do not interfere with TF or SRP binding to translating ribosomes, indicating that nascent-chain processing can take place before or in parallel with TF or SRP binding.