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01000caa a22002652 4500 |
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NLM17277019X |
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DE-627 |
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20250208152444.0 |
| 007 |
tu |
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231223s2007 xx ||||| 00| ||eng c |
| 028 |
5 |
2 |
|a pubmed25n0576.xml
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|a (DE-627)NLM17277019X
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| 035 |
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|a (NLM)17766005
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Ristic, Zoran
|e verfasserin
|4 aut
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| 245 |
1 |
0 |
|a Chloroplast protein synthesis elongation factor, EF-Tu, reduces thermal aggregation of rubisco activase
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| 264 |
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1 |
|c 2007
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| 336 |
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|a Text
|b txt
|2 rdacontent
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| 337 |
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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| 338 |
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|a Band
|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 30.01.2008
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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| 520 |
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|a Chloroplast protein synthesis elongation factor, EF-Tu, has been implicated in heat tolerance in maize. The recombinant precursor of this protein, pre-EF-Tu, has been found to exhibit chaperone activity and protect heat-labile proteins, such as citrate synthase and malate dehydrogenase, from thermal aggregation. Chloroplast EF-Tu is highly conserved and it is possible that the chaperone activity of this protein is not species-specific. In this study, we investigated the effect of native wheat pre-EF-Tu on thermal aggregation of rubisco activase. Additionally, we investigated the effect of native and recombinant maize pre-EF-Tu on activase aggregation. Activase was chosen because it displays an exceptional sensitivity to thermal aggregation and constrains photosynthesis at high temperature. The native precursors of both wheat and maize EF-Tu displayed chaperone activity, as shown by the capacity of both proteins to reduce thermal aggregation of rubisco activase in vitro. Similarly, the recombinant maize pre-EF-Tu protected activase from thermal aggregation. This is the first report on chaperone activity of native pre-EF-Tu and the first evidence for thermal protection of a photosynthetic enzyme by this putative chaperone. The results are consistent with the hypothesis that chloroplast EF-Tu plays a functional role in heat tolerance by acting as a molecular chaperone
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| 650 |
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4 |
|a Journal Article
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| 650 |
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7 |
|a Plant Proteins
|2 NLM
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| 650 |
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7 |
|a Protein Precursors
|2 NLM
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| 650 |
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7 |
|a Recombinant Proteins
|2 NLM
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| 650 |
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7 |
|a rca protein, plant
|2 NLM
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| 650 |
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7 |
|a Peptide Elongation Factor Tu
|2 NLM
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| 650 |
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7 |
|a EC 3.6.1.-
|2 NLM
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| 700 |
1 |
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|a Momcilović, Ivana
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Fu, Jianming
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Callegari, Eduardo
|e verfasserin
|4 aut
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| 700 |
1 |
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|a DeRidder, Benjamin P
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 164(2007), 12 vom: 13. Dez., Seite 1564-71
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnns
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| 773 |
1 |
8 |
|g volume:164
|g year:2007
|g number:12
|g day:13
|g month:12
|g pages:1564-71
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| 912 |
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|a GBV_USEFLAG_A
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| 912 |
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|a SYSFLAG_A
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| 912 |
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|a GBV_NLM
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| 912 |
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|a GBV_ILN_350
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| 951 |
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|a AR
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| 952 |
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|d 164
|j 2007
|e 12
|b 13
|c 12
|h 1564-71
|