1986
DOI: 10.1016/0076-6879(86)18080-3
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Purification of chloroplast elongation factors

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Cited by 4 publications
(3 citation statements)
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“…The results showed that the two proteins involved in translation process were downregulated; the putative elongation factor 3 (EF-3) (PHATRDRAFT_27838), which facilitates EF-1-alpha-dependent binding with aminoacyl-tRNA to the ribosome, thus resulting in the transduction of mechanical energy from nucleoside triphosphate energy for translocation during translation 57 and chloroplast elongation factor Ts, (EFTS_PHATC), which associates with the EF-Tu-GDP complex and remains bound to the aminoacyl-tRNA, thus facilitating the conversion of GDP to GTP 58 . This showed that the translation levels of proteins decreased after 48 h of –P starvation.…”
Section: Resultsmentioning
confidence: 99%
“…The results showed that the two proteins involved in translation process were downregulated; the putative elongation factor 3 (EF-3) (PHATRDRAFT_27838), which facilitates EF-1-alpha-dependent binding with aminoacyl-tRNA to the ribosome, thus resulting in the transduction of mechanical energy from nucleoside triphosphate energy for translocation during translation 57 and chloroplast elongation factor Ts, (EFTS_PHATC), which associates with the EF-Tu-GDP complex and remains bound to the aminoacyl-tRNA, thus facilitating the conversion of GDP to GTP 58 . This showed that the translation levels of proteins decreased after 48 h of –P starvation.…”
Section: Resultsmentioning
confidence: 99%
“…EF-Tu is an abundant soluble protein and has been purified from spinach [ 31 ] and Euglena gracilis [30]. Hybridization analysis using the E. coli EF-Tu gene (tufA) first suggested the existence of a gene encoding chloroplast EF-Tu in the chloroplast genome of Chlamydomonas reinhardtii [33].…”
Section: Introductionmentioning
confidence: 99%
“…However, higher plant chloroplast EF-Tu, which shows higher sequence homology to bacterial elongation factor than to cytoplasmic elongation factor, is encoded by nuclear DNA (Baldauf and Palmer, 1990;Baldauf et al, 1990;Bonny and Stutz, 1993). Chloroplast EF-Tu is an abundant soluble protein and has been purified from spinach (Tiboni et al, 1978), E. gracilis (Tiboni and Ciferri, 1986), and Nicotiana tabacum (Murayama et al, 1993). A single nuclear tufA gone was identified in Arabidopsis thaliana (Baldauf and Palmer, 1990) and multiple copies of this gene seemed to exist in the nuclear genome of other Brassicaceae (Baldauf et al, 1990).…”
mentioning
confidence: 98%