Distribution of the early light‐inducible protein in the thylakoids of developing pea chloroplasts

Cronshagen, Udo; Herzfeld, Frank

doi:10.1111/j.1432-1033.1990.tb19347.x

Cited by 16 publications

(9 citation statements)

References 27 publications

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“…Integration of ELIP species, in contrast to the processing step, is almost temperature independent over 0-30°C. From the fact that a temperature above 35°C does not lead to an increase in the integration of ELIP, we tend to conclude that integration into the thylakoid membrane occurs in the stromal region, as was found in vivo [6] and after posttranslational transport [7].…”

Section: Discussionmentioning

confidence: 94%

Integration of early light‐inducible proteins into isolated thylakoid membranes

Kruse

Kloppstech

1992

European Journal of Biochemistry

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An in-vitro system has been established to study the integration of early light-inducible proteins (ELIP) into isolated thylakoid membranes. The in-vitro-expressed ELIP precursor proteins exist in two forms, a high-molecular-mass aggregate which is accessible to trypsin but no longer to the stromal processing protease and a soluble form which is readily cleaved to the mature form by the stromal protease. The mature form of ELIP is integrated into thylakoid membranes; its correct integration can be deduced from the observation that the posttranslationally transported products and the invitro integrated ELIP species are cleaved by trypsin to products of the same apparent molecular mass. Trypsin-resistant fragments of high-molecular-mass and low-molecular-mass ELIP appear to have the same size. The processed ELIP species, as well as an engineered mature form of ELIP, are integrated into isolated thylakoid membranes. Integration of the mature protein occurs in the absence of stroma, into sodium-chloride-washed, and trypsin-treated thylakoid membranes. The process of integration is almost temperature independent over 0 -30 "C. Analysis of the time course ofintegration leads to the conclusion that, under in-vitro conditions, processing but not integration into membranes is the rate-limiting step. In the absence of stroma, the ELIP precursor is bound to the thylakoid membranes, however, it is no longer accessible to the stromal maturating protease when added after binding has occurred. In conclusion, integration of ELIP differs in many essential details from that of its relatives, the light-harvesting chlorophyll u/b protein family.Early light-inducible proteins (ELIP) are short lived, thylakoid-membrane-located proteins whose genes are transiently transcribed after illumination of etiolated pea [l] or barley plantlets [2, 31. Whilc, to date, only one protein has been found in pea [l, 41, two small multigene families of different size have been characterized in barley [2].The expression of ELIP genes is not restricted to etiolated plantlets as their genes are transcribed in green plants early in the morning and under the control of the circadian clock [5]. Both in vivo [6] and after in-vitro import into intact chloroplasts [I, 71, ELIP species are integrated into the thylakoid membranes. By means of detergent fractionation of cross-linked thylakoid membranes, we found that ELIP species are associated with a preparation of photosystem-I1 (PS 11) particles [7, 81 and, in particular, with the D1 protein.D1, as a constituent of PS 11, has been found prevalently in the grana thylakoid membrane fraction [9], while a considerable portion of ELIP is obtained from the stroma thylakoid membranes [6, 71 and the intermediate membrane preparations [7]. These findings indicate that the association of EIJP with PS I1 should be confined to the site of insertion of preDl into the PS I1 particles [lo].The turnover and, consequently, the integration of D1 is accelerated after damage of PS I1 reaction centers due to highlight stress, a...

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Section: Discussionmentioning

confidence: 94%

Integration of early light‐inducible proteins into isolated thylakoid membranes

Kruse

Kloppstech

1992

European Journal of Biochemistry

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“…Elip proteins appear transiently during greening of etiolated seedlings in higher plants and disappear before chloroplast development is completed (Meyer and Kloppstech, 1984;Scharnhorst et al, 1985;Grimm and Kloppstech, 1987;Kolanus et al, 1987;Grimm et al, 1989). They are synthesized as precursor proteins and transported into chloroplasts, where they have been found associated with both photosystems I and II (Adamska and Kloppstech, 1991;Cronshagen and Herzfeld, 1990). A role in the assembly of the photosystem or in the integration of pigments into the mature pigment-protein complexes has been suggested.…”

Section: Discussionmentioning

confidence: 99%

A desiccation-related Elip-like gene from the resurrection plant Craterostigma plantagineum is regulated by light and ABA.

et al. 1992

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The resurrection plant Craterostigma plantagineum tolerates an extreme loss of cellular water. Therefore this plant is being studied as model system to analyse desiccation tolerance at the molecular level. Upon dehydration, new transcripts are abundantly expressed in different tissues of the plant. One such desiccation‐related nuclear gene (dsp‐22 for desiccation stress protein) encodes a mature 21 kDa protein which accumulates in the chloroplasts. Sequence analysis indicates that dsp‐22 is closely related to early light inducible genes (Elip) of higher plants and to a carotene biosynthesis related gene (cbr) isolated from the green alga Dunaliella bardawil. In contrast to other desiccation‐related genes, light is an essential positive factor regulating the expression of dsp‐22: ABA‐mediated gene activation leads to the accumulation of the transcript only in the presence of light. During the desiccation process, light acts at the transcriptional and post‐transcriptional levels. The implications of these different controls and the possible role of the dsp‐22 protein in the desiccation/rehydration process are discussed.

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“…The transcripts and the corresponding proteins are induced during the first hours of greening of etiolated seedlings (Grimm and Kloppstech, 1987;Cronshagen and Herzfeld, 1990;Pötter and Kloppstech, 1993), when the developing photosynthetic apparatus is very susceptible to photooxidation (Caspi et al, 2000). In mature plants they are absent until the plants are exposed to photoinhibitory conditions, such as high light (Adamska et al, 1992b;Pö tter and Kloppstech, 1993), high light and cold (Montané et al, 1997), high salinity (Sävenstrand et al, 2004), UV-B irradiance (Adamska et al, 1992a), or desiccation (Zeng et al, 2002).…”

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confidence: 99%

Suppression of Both ELIP1 and ELIP2 in Arabidopsis Does Not Affect Tolerance to Photoinhibition and Photooxidative Stress

et al. 2006

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ELIPs (early light-induced proteins) are thylakoid proteins transiently induced during greening of etiolated seedlings and during exposure to high light stress conditions. This expression pattern suggests that these proteins may be involved in the protection of the photosynthetic apparatus against photooxidative damage. To test this hypothesis, we have generated Arabidopsis (Arabidopsis thaliana) mutant plants null for both elip genes (Elip1 and Elip2) and have analyzed their sensitivity to light during greening of seedlings and to high light and cold in mature plants. In particular, we have evaluated the extent of damage to photosystem II, the level of lipid peroxidation, the presence of uncoupled chlorophyll molecules, and the nonphotochemical quenching of excitation energy. The absence of ELIPs during greening at moderate light intensities slightly reduced the rate of chlorophyll accumulation but did not modify the extent of photoinhibition. In mature plants, the absence of ELIP1 and ELIP2 did not modify the sensitivity to photoinhibition and photooxidation or the ability to recover from light stress. This raises questions about the photoprotective function of these proteins. Moreover, no compensatory accumulation of other ELIP-like proteins (SEPs, OHPs) was found in the elip1/elip2 double mutant during high light stress. elip1/elip2 mutant plants show only a slight reduction in the chlorophyll content in mature leaves and greening seedlings and a lower zeaxanthin accumulation in high light conditions, suggesting that ELIPs could somehow affect the stability or synthesis of these pigments. On the basis of these results, we make a number of suggestions concerning the biological function of ELIPs.

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Distribution of the early light‐inducible protein in the thylakoids of developing pea chloroplasts

Cited by 16 publications

References 27 publications

Integration of early light‐inducible proteins into isolated thylakoid membranes

Integration of early light‐inducible proteins into isolated thylakoid membranes

A desiccation-related Elip-like gene from the resurrection plant Craterostigma plantagineum is regulated by light and ABA.

Suppression of Both ELIP1 and ELIP2 in Arabidopsis Does Not Affect Tolerance to Photoinhibition and Photooxidative Stress

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