Heat Shock Proteins Partially Protect Against Photoinhibition of Chlamydomonas Reinhardtii During Heat Shock

Schuster, Gadi; Even, Dena; Kloppstech, Klaus; Ohad, Itzhak

doi:10.1007/978-94-017-0519-6_17

Cited by 4 publications

(4 citation statements)

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“…So far the mechanism of the binding is obscure. The data indicate that the 22-kDa and the 25-kDa proteins are not integral parts of one of the multiprotein complexes of the thylakoid membrane, although there is evidence that the 22-kDa protein of Chlumydomonas has a protective effect on the PSII complex [24]. Low concentrations of Triton X-100 which do not interfere with the core complexes of PSI and PSII [25] readily remove the two HSP from the membranes at least after in vitro protein transport.…”

Section: Discussionmentioning

confidence: 99%

“…It has been observed in Chlumydomonus [24] that the damage by heat as far as the integrity of the photosynthetic apparatus is concerned is much more severe in the light than in the dark. The light intensities that caused damage in these experiments are easily tolerated under normal growth temperatures.…”

Section: The Influence Of Light Intensity During Heat Shock On the Bimentioning

confidence: 99%

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Temperature‐dependent binding to the thylakoid membranes of nuclear‐coded chloroplast heat‐shock proteins

Glaczinski

Kloppstech

1988

European Journal of Biochemistry

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Two nuclear-coded heat-shock proteins (HSP) of pea (Pisum sativum) are synthesized as larger precursors of 26 kDa and 30 kDa in vitro. They are transported post-translationally into isolated, homologous chloroplasts where they are processed to mature proteins of 22 kDa and 25 kDa, respectively. When the chloroplasts used for the transport are isolated from control plants grown at 25°C the 22-kDa and 25-kDa HSPs are located in the stroma of the chloroplasts. However, when chloroplasts are prepared from heat-shocked plants both proteins are found bound to the thylakoid membranes. The transition of the non-binding to the binding status is comparatively sharp and occurs between 36°C and 40°C in the variety 'Rosa Krone'. The transition temperature has been determined at 38 "C for 'Rosa Krone' and at 40 "C for the variety 'Golf. At 42 "C, 15-min treatment of the plants is sufficient to induce membrane binding, which persists for at least 4-6 h (but not for 24 h) after return to the ambient temperature. Once lost, membrane binding can be reinduced by a second heat-shock treatment in vivo. High light intensities during the heat shock interfere with the binding capacity for heat-shock proteins.All prokaryotic and eukaryotic organisms that have so far been investigated respond to a sudden sublethal rise in temperature by the transient expression of a small number of proteins ranging in size from 16 kDa to 110 kDa [I]. This response is regulated both at the level of transcription [2] and translation [3,4] and is believed to protect against heat damage [5, 61. It is evident that plants have no chance to avoid a heatshock by movement, therefore a protective mechanism against heat damage should be essential for plant survival; furthermore, in nature the heat stress will in most cases be accompanied by rather high light intensities and, in semi-arid zones or at noon time, in addition by a lack of water. Despite these facts the interest in the investigation of the heat-shock response in plants is quite recent [7, 81. Both the molecular mechanisms by which plants respond to heat shock as well as the molecular mass range of plant heat-shock proteins and the primary structures of the proteins show high analogy to the heat-shock response system of animals. An obvious exception, which seems to be specific for higher plants, is the occurrence of multigene families of rather small proteins of 16-18 kDa [9, 101. Another peculiarity of plants are chloroplast heat-shock proteins of 22 kDa and 25 kDa, discovered in this laboratory [ l l , 121 and independently and almost simultaneously by two other groups [13, 141. According to these findings, the chloroplast heat-shock proteins derive from nuclear-coded precursor proteins which are synthesized on cytosolic ribosomes and transported into the chloroplasts. The exception is the 22-kDa heat-shock protein (HSP) from Chlamydomonas for which no precursor has been found [ll]. It is interesting to note in this connection that so far only in the alga Acetabularia has evidence for chloroplast DNA...

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Section: Discussionmentioning

confidence: 99%

Section: The Influence Of Light Intensity During Heat Shock On the Bimentioning

confidence: 99%

Temperature‐dependent binding to the thylakoid membranes of nuclear‐coded chloroplast heat‐shock proteins

Glaczinski

Kloppstech

1988

European Journal of Biochemistry

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“…Induction of the synthesis of HSPs has been reported to occur in the presence of stress factors other than heat stress (Ho and Sachs, 1989). A subset of HSPs, of 21 to 28 kD, are localized in the chloroplast, where they are either soluble (Vierling et al, 1986) or associated with the thylakoid membrane (Schuster et al, 1987). It has been proposed that thylakoid-associated HSPs may serve to protect PSII from damage due to stress (Schuster et al, 1987).…”

Section: Discussionmentioning

confidence: 99%

“…A subset of HSPs, of 21 to 28 kD, are localized in the chloroplast, where they are either soluble (Vierling et al, 1986) or associated with the thylakoid membrane (Schuster et al, 1987). It has been proposed that thylakoid-associated HSPs may serve to protect PSII from damage due to stress (Schuster et al, 1987). It is intriguing to note that a 70-kD HSP is observed in maize (Ho and Sachs, 19891, and that an increase in a 69-kD polypeptide was observed in both the soluble and membrane fractions, but not in the thylakoid fraction, in response to O,.…”

Section: Discussionmentioning

confidence: 99%

Ozone-Induced Alterations in the Accumulation of Newly Synthesized Proteins in Leaves of Maize

Pino¹,

Mudd²,

Bailey‐Serres³

1995

Plant Physiol.

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We examined the response of leaves of 3-week-old maize (Zea mays 1.) t o short-term (5 h) fumigation with O,-enriched air (O, 0.12, 0.24, or Tropospheric O, is a major component of photochemical air pollution and has phytotoxic effects on vegetation, including decreased photosynthesis, leaf injury, reduced growth of shoots and roots, accelerated senescence, and reduced crop yield (Heck et al., 1988; Heagle, 1989). Levels of tropospheric O, range from 0.02 to 0.05 pL/L in unpolluted areas to as high as 0.40 pL/L in the most polluted urban environments (Seinfeld, 1989). Plant resistance to elevated O, levels can result from either avoidance or tolerance mechanisms (Taylor, 1978). Avoidance involves the physical exclusion of pollutants from the plant such as through stomatal closure. Tolerance can result from avoidance and/or biochemical responses such as increased detoxification and repair processes or induction of biochem-

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Developmental Physiology

Hock¹

1989

Progress in Botany

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Heat Shock Proteins Partially Protect Against Photoinhibition of Chlamydomonas Reinhardtii During Heat Shock

Cited by 4 publications

References 9 publications

Temperature‐dependent binding to the thylakoid membranes of nuclear‐coded chloroplast heat‐shock proteins

Temperature‐dependent binding to the thylakoid membranes of nuclear‐coded chloroplast heat‐shock proteins

Ozone-Induced Alterations in the Accumulation of Newly Synthesized Proteins in Leaves of Maize

Developmental Physiology

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