Document Detail

The protein synthesis machinery operates at the same expense in eurythermal and cold stenothermal pectinids.
MedLine Citation:
PMID:  12695984     Owner:  NLM     Status:  MEDLINE    
Translationally active cell-free systems from gills of the Antarctic scallop Adamussium colbecki and the European scallop Aequipecten opercularis were developed, characterised, and optimised for an analysis of translational capacity. The aim was to determine the energetic cost of protein synthesis in the in vitro cell-free system by directly measuring the required energy equivalents in the lysates. Protein synthesis rate in assays conducted with lysates of A. colbecki (1.029+/-0.061 micromol Phe min(-1) at 15 degrees C; Phe=phenylalanine) were higher compared with lysates of A. opercularis (0.087+/-0.013 micromol Phe min(-1) at 15 degrees C and 0.156+/-0.023 micromol Phe min(-1) at 25 degrees C). This can in part be attributed to the naturally occurring higher RNA content in lysates of A. colbecki (0.883+/-0.037 mg RNA mL(-1) lysate) compared with A. opercularis (0.468+/-0.013 mg RNA mL(-1) lysate). There was no significant difference in the energetic costs of protein synthesis in cell-free systems of gill lysates of the cold stenothermal A. colbecki with 4.3+/-0.7 energy equivalents per peptide bond formed and the eurythermal A. opercularis with 5.6+/-0.6 energy equivalents, indicating that there are no differences in the efficiency of the translation machinery. The energetic costs specified for protein synthesis correspond with the generally accepted theoretical value of four energy equivalents per peptide bond formed, especially in gill lysates of A. colbecki, whereas the value for gill lysates of A. opercularis was slightly higher.
Daniela Storch; Hans O Pörtner
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Physiological and biochemical zoology : PBZ     Volume:  76     ISSN:  1522-2152     ISO Abbreviation:  Physiol. Biochem. Zool.     Publication Date:    2003 Jan-Feb
Date Detail:
Created Date:  2003-04-15     Completed Date:  2003-09-02     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  100883369     Medline TA:  Physiol Biochem Zool     Country:  United States    
Other Details:
Languages:  eng     Pagination:  28-40     Citation Subset:  IM    
Alfred Wegener Institute for Polar and Marine Research, Columbusstrasse, D-27568 Bremerhaven, Germany.
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MeSH Terms
Adenosine Triphosphate / metabolism
Cold Temperature*
Energy Metabolism*
Gills / chemistry,  physiology
Guanosine Triphosphate / metabolism
Mollusca / physiology*
Oceans and Seas
Phenylalanine / metabolism
Protein Biosynthesis / physiology*
Proteins / metabolism
Reg. No./Substance:
0/Proteins; 56-65-5/Adenosine Triphosphate; 63-91-2/Phenylalanine; 86-01-1/Guanosine Triphosphate

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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