ELIPs - Light-induced stress proteins
First-pass extracted concept
ELIPs
Candidate: toolkit item2 source documents5 linked claims
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Aliases
early light-induced proteins, light-induced stress proteins, Light-induced stress proteins
Evidence Snippets
Supporting Sources
Linked Claims
ELIPs can bind chlorophyll a and lutein.
Quoted textsource-backed
Isolation of ELIPs in a native form and analysis of pigments bound to these proteins revealed that ELIPs can bind chlorophyll a and lutein.
Accumulation of ELIPs under light stress is correlated with photoinactivation of PSII, degradation of the D1 protein of the PSII reaction centre, and changes in pigment levels.
Quoted textsource-backed
The accumulation of ELIPs under light stress conditions is correlated with the photoinactivation of PSII, degradation of the D l ‐protein of PSII reaction centre and changes in the level of pigments.
ELIPs might be unique chlorophyll-binding proteins with transient functions during light stress, including a postulated transient pigment-carrier function.
Quoted textsource-backed
These data indicate that ELIPs might represent unique chlorophyll‐binding proteins which have a transient function(s) during light stress. A transient ‘pigment‐carrier’ function is postulated for ELIPs.
ELIPs are considered part of chloroplast protective responses under light stress conditions.
Quoted textsource-backed
The induction of specific light stress proteins, the ELIPs (for early light‐induced proteins) can be considered to be part of these protective responses.
Accumulation of ELIPs in thylakoids is strictly controlled by pigment content, especially chlorophylls.
Quoted textsource-backed
Futhermore, the accumulation of ELIPs in the thylakoids is strictly controlled by the pigment content, especially by chlorophylls.