In vitro chloroplast protein synthesis by the chromophytic alga Olisthodiscus luteus

Biochemistry ◽  
1985 ◽  
Vol 24 (10) ◽  
pp. 2550-2556 ◽  
Author(s):  
Michael E. Reith ◽  
Rose Ann Cattolico
Keyword(s):  
Protein Synthesis ◽  
Chloroplast Protein ◽  
Olisthodiscus Luteus ◽  
Chromophytic Alga ◽  
Chloroplast Protein Synthesis

Heat-stress induced synthesis of chloroplast protein synthesis elongation factor (EF-Tu) in a heat-tolerant maize line

Planta ◽  
2001 ◽  
Vol 212 (3) ◽  
pp. 359-366 ◽  
Author(s):  
Shailendra K. Bhadula ◽  
Thomas E. Elthon ◽  
Jeffrey E. Habben ◽  
Timothy G. Helentjaris ◽  
Shuping Jiao ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Heat Stress ◽  
Elongation Factor ◽  
Maize Line ◽  
Chloroplast Protein ◽  
Heat Tolerant ◽  
Chloroplast Protein Synthesis

Processing of the precursor to a chloroplast ribosomal protein made in the cytosol occurs in two steps, one of which depends on a protein made in the chloroplast

1985 ◽  
Vol 5 (5) ◽  
pp. 1093-1099
Author(s):  
R J Schmidt ◽  
N W Gillham ◽  
J E Boynton
Keyword(s):  
Molecular Weight ◽  
Protein Synthesis ◽  
Ribosomal Protein ◽  
Apparent Molecular Weight ◽  
Protein L ◽  
Mature Form ◽  
Chloroplast Protein Synthesis ◽  
Made In

In pulse-chase experiments in which log-phase cells of Chlamydomonas reinhardtii were labeled in vivo for 5 min with H2(35)SO4, fluorographs of immunoprecipitates from whole cell extracts revealed that chloroplast ribosomal proteins L-2, L-6, L-21, and L-29, which are made in the cytosol and imported, appeared in their mature forms. However, in the case of chloroplast ribosomal protein L-18, which is also made in the cytoplasm and imported, a prominent precursor with an apparent molecular weight of 17,000 was found at the end of a 5-min pulse. This precursor was processed to its mature size (apparent molecular weight of 15,500) within the first 5 min of the subsequent chase. As determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the precursor to L-18 formed in vivo was 1.5 kilodaltons smaller than the primary product detected in translations of Chlamydomonas polyadenylated RNA in vitro. Upon a 10-min incubation with a postribosomal supernatant from Chlamydomonas, the 18,500-dalton precursor detected in vitro could be partially converted into a polypeptide that comigrated with the 17,000-dalton precursor detected in extracts of cells labeled in vivo. Under conditions in which the total amounts of chloroplast proteins had been reduced and cells were made to synthesize ribosomes rapidly, the apparent half-life of the 17,000-dalton precursor was extended over that seen in log-phase cells. When chloroplast protein synthesis was inhibited with lincomycin for 3 h before labeling under these conditions, the 17,000-dalton L-18 precursor but not the mature form was found, and the precursor was slowly degraded during a 60-min chase. When cells were placed in the dark for 3 h before labeling, processing of this precursor to the mature form appeared unaffected, but the chloroplast-synthesized ribosomal protein L-26 was detected, indicating that chloroplast protein synthesis was still occurring. We interpret these results to indicate that the maturation of protein L-18 in vivo involves at least two processing steps, one of which depends on a protein made on chloroplast ribosomes.

Chloroplast protein synthesis

Nature ◽  
1975 ◽  
Vol 254 (5495) ◽  
pp. 13-13 ◽  
Author(s):  
Harry Smith
Keyword(s):  
Protein Synthesis ◽  
Chloroplast Protein ◽  
Chloroplast Protein Synthesis

Chaperone activity of recombinant maize chloroplast protein synthesis elongation factor, EF-Tu

2004 ◽  
Vol 271 (18) ◽  
pp. 3684-3692 ◽  
Author(s):  
Damodara Rao ◽  
Ivana Momcilovic ◽  
Satoru Kobayashi ◽  
Eduardo Callegari ◽  
Zoran Ristic
Keyword(s):  
Protein Synthesis ◽  
Elongation Factor ◽  
Chaperone Activity ◽  
Chloroplast Protein ◽  
Maize Chloroplast ◽  
Chloroplast Protein Synthesis
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