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Euglena gracilis chloroplast initiation factor 2. Identification and initial characterization.

J C Gold, L L Spremulli

The Journal of Biological Chemistry

|December 5, 1985

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The chloroplast protein synthesis factor (IF-2chl) binds fMet-tRNAMeti to Euglena gracilis chloroplast ribosomes. This factor is more abundant in light-grown cells and requires GTP for optimal activity.

Area of Science:

Chloroplast biology
Molecular biology
Protein synthesis

Background:

Chloroplasts possess their own protein synthesis machinery, distinct from the cytoplasm.
Initiation factors are crucial for the first step of translation, binding the initiator tRNA to the ribosome.

Purpose of the Study:

To identify and characterize the chloroplast protein synthesis initiation factor (IF-2chl) in Euglena gracilis.
To investigate the properties and regulation of IF-2chl activity.

Main Methods:

Extraction and partial purification of IF-2chl from Euglena gracilis cell extracts using phosphocellulose chromatography.
Assay of IF-2chl activity by measuring the binding of fMet-tRNAMeti to chloroplast 30 S ribosomal subunits.
Investigating the effects of GTP, cations, and other initiation factors (E. coli IF-1, IF-3) on the binding reaction.

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Main Results:

IF-2chl was identified and partially purified, separating it from the cytoplasmic factor eIF-2A.
IF-2chl activity was significantly higher in light-grown versus dark-grown cells, with most activity in the postribosomal supernatant.
The binding reaction was message-dependent, stimulated by GTP, and showed broad cation optima. IF-2chl activity was enhanced by E. coli IF-1 and IF-3.
Chloroplast IF-2 showed high activity on homologous subunits but low activity on prokaryotic or eukaryotic subunits.

Conclusions:

IF-2chl is a key factor for initiating protein synthesis on Euglena chloroplast ribosomes.
Light-dependent regulation of IF-2chl suggests a link between chloroplast biogenesis and protein synthesis.
IF-2chl exhibits characteristics similar to prokaryotic initiation factors but is specific for chloroplast ribosomes.