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Calcium-Dependent Interaction of Calmodulin with Human 80S Ribosomes and Polyribosomes.

Behnen, Petra LU ; Davis, Elizabeth; Delaney, Erin; Frohm, Birgitta LU ; Bauer, Mikael LU ; Cedervall, Tommy LU ; O'Connell, David; Akerfeldt, Karin S and Linse, Sara LU (2012) In Biochemistry 51(34). p.6718-6727
Abstract
Ribosomes are the protein factories of every living cell. The process of protein translation is highly complex and tightly regulated by a large number of diverse RNAs and proteins. Earlier studies indicate that Ca(2+) plays a role in protein translation. Calmodulin (CaM), a ubiquitous Ca(2+)-binding protein, regulates a large number of proteins participating in many signaling pathways. Several 40S and 60S ribosomal proteins have been identified to interact with CaM, and here, we report that CaM binds with high affinity to 80S ribosomes and polyribosomes in a Ca(2+)-dependent manner. No binding is observed in buffer with 6 mM Mg(2+) and 1 mM EGTA that chelates Ca(2+), suggesting high specificity of the CaM-ribosome interaction dependent on... (More)
Ribosomes are the protein factories of every living cell. The process of protein translation is highly complex and tightly regulated by a large number of diverse RNAs and proteins. Earlier studies indicate that Ca(2+) plays a role in protein translation. Calmodulin (CaM), a ubiquitous Ca(2+)-binding protein, regulates a large number of proteins participating in many signaling pathways. Several 40S and 60S ribosomal proteins have been identified to interact with CaM, and here, we report that CaM binds with high affinity to 80S ribosomes and polyribosomes in a Ca(2+)-dependent manner. No binding is observed in buffer with 6 mM Mg(2+) and 1 mM EGTA that chelates Ca(2+), suggesting high specificity of the CaM-ribosome interaction dependent on the Ca(2+) induced conformational change of CaM. The interactions between CaM and ribosomes are inhibited by synthetic peptides comprising putative CaM-binding sites in ribosomal proteins S2 and L14. Using a cell-free in vitro translation system, we further found that these synthetic peptides are potent inhibitors of protein synthesis. Our results identify an involvement of CaM in the translational activity of ribosomes. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemistry
volume
51
issue
34
pages
6718 - 6727
publisher
The American Chemical Society
external identifiers
  • wos:000307988600002
  • pmid:22856685
  • scopus:84867514168
ISSN
0006-2960
DOI
10.1021/bi3005939
language
English
LU publication?
yes
id
182e4926-2f98-49c9-9eb2-af33c4324bab (old id 3047806)
date added to LUP
2012-09-10 15:42:36
date last changed
2017-01-01 03:35:26
@article{182e4926-2f98-49c9-9eb2-af33c4324bab,
  abstract     = {Ribosomes are the protein factories of every living cell. The process of protein translation is highly complex and tightly regulated by a large number of diverse RNAs and proteins. Earlier studies indicate that Ca(2+) plays a role in protein translation. Calmodulin (CaM), a ubiquitous Ca(2+)-binding protein, regulates a large number of proteins participating in many signaling pathways. Several 40S and 60S ribosomal proteins have been identified to interact with CaM, and here, we report that CaM binds with high affinity to 80S ribosomes and polyribosomes in a Ca(2+)-dependent manner. No binding is observed in buffer with 6 mM Mg(2+) and 1 mM EGTA that chelates Ca(2+), suggesting high specificity of the CaM-ribosome interaction dependent on the Ca(2+) induced conformational change of CaM. The interactions between CaM and ribosomes are inhibited by synthetic peptides comprising putative CaM-binding sites in ribosomal proteins S2 and L14. Using a cell-free in vitro translation system, we further found that these synthetic peptides are potent inhibitors of protein synthesis. Our results identify an involvement of CaM in the translational activity of ribosomes.},
  author       = {Behnen, Petra and Davis, Elizabeth and Delaney, Erin and Frohm, Birgitta and Bauer, Mikael and Cedervall, Tommy and O'Connell, David and Akerfeldt, Karin S and Linse, Sara},
  issn         = {0006-2960},
  language     = {eng},
  number       = {34},
  pages        = {6718--6727},
  publisher    = {The American Chemical Society},
  series       = {Biochemistry},
  title        = {Calcium-Dependent Interaction of Calmodulin with Human 80S Ribosomes and Polyribosomes.},
  url          = {http://dx.doi.org/10.1021/bi3005939},
  volume       = {51},
  year         = {2012},
}