Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-194 |
Sentence |
denotes |
Heterologous expression of moss light-harvesting complex stress-related 1 (LHCSR1), the chlorophyll a-xanthophyll pigment-protein complex catalyzing non-photochemical quenching, in Nicotiana sp. |
T2 |
195-349 |
Sentence |
denotes |
Oxygenic photosynthetic organisms evolved mechanisms for thermal dissipation of energy absorbed in excess to prevent formation of reactive oxygen species. |
T3 |
350-665 |
Sentence |
denotes |
The major and fastest component, called non-photochemical quenching, occurs within the photosystem II antenna system by the action of two essential light-harvesting complex (LHC)-like proteins, photosystem II subunit S (PSBS) in plants and light-harvesting complex stress-related (LHCSR) in green algae and diatoms. |
T4 |
666-760 |
Sentence |
denotes |
In the evolutionary intermediate Physcomitrella patens, a moss, both gene products are active. |
T5 |
761-882 |
Sentence |
denotes |
These proteins, which are present in low amounts, are difficult to purify, preventing structural and functional analysis. |
T6 |
883-1080 |
Sentence |
denotes |
Here, we report on the overexpression of the LHCSR1 protein from P. patens in the heterologous systems Nicotiana benthamiana and Nicotiana tabacum using transient and stable nuclear transformation. |
T7 |
1081-1366 |
Sentence |
denotes |
We show that the protein accumulated in both heterologous systems is in its mature form, localizes in the chloroplast thylakoid membranes, and is correctly folded with chlorophyll a and xanthophylls but without chlorophyll b, an essential chromophore for plants and algal LHC proteins. |
T8 |
1367-1551 |
Sentence |
denotes |
Finally, we show that recombinant LHCSR1 is active in quenching in vivo, implying that the recombinant protein obtained is a good material for future structural and functional studies. |