Protein Metabolism in Senescing Wheat Leaves

Lamattina, Lorenzo; Lezica, Rafael Pont; Conde, Rubén D.

doi:10.1104/pp.77.3.587

Cited by 25 publications

(11 citation statements)

References 19 publications

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“…process during senescence and to a lesser extent by a decrease in protein synthetic capacity (Lamattina et al, 1985). It seems that the senescence-specific increase in proteolytic activities does not affect ELIP protein levels.…”

Section: Discussionmentioning

confidence: 94%

Expression of Early Light-Inducible Proteins in Flag Leaves of Field-Grown Barley

1994

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Section: Discussionmentioning

confidence: 94%

Expression of Early Light-Inducible Proteins in Flag Leaves of Field-Grown Barley

1994

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“…The protease activities involved in the degradation of Rubisco have long been a major objective of senescence studies (Friedrich & Huffaker 1980; Lamattina et al. 1985).…”

Section: Dismantling Of the Photosynthetic Apparatus And Chloroplast mentioning

confidence: 99%

“…The protease activities involved in the degradation of Rubisco have long been a major objective of senescence studies (Friedrich & Huffaker 1980;Lamattina et al 1985). In flag leaves of wheat, a biphasic degradation of Rubisco has been observed during grain filling (Peoples et al 1980).…”

Section: Dismantling Of the Photosynthetic Apparatus And Chloroplast mentioning

confidence: 99%

Leaf senescence and nutrient remobilisation in barley and wheat

Gregersen¹,

Holm²,

2008

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Extensive studies have been undertaken on senescence processes in barley and wheat and their importance for the nitrogen use efficiency of these crop plants. During the senescence processes, proteins are degraded and nutrients are re‐mobilised from senescing leaves to other organs, especially the developing grain. Most of the proteins degraded reside in the chloroplasts, with Rubisco constituting the most dominant protein fraction. Despite intensive studies, the proteases responsible for Rubisco degradation have not yet been identified. Evidence for degradation of stromal proteins outside of chloroplasts is summarised. Rubisco is thought to be released from chloroplasts into vesicles containing stroma material (RCB = Rubisco‐containing bodies). These vesicles may then take different routes for their degradation. Transcriptome analyses on barley and wheat senescence have identified genes involved in degradative, metabolic and regulatory processes that could be used in future strategies aimed at modifying the senescence process. The breeding of crops for characters related to senescence processes, e.g. higher yields and better nutrient use efficiency, is complex. Such breeding has to cope with the dilemma that delayed senescence, which could lead to higher yields, is correlated with a decrease in nutrient use efficiency. Pinpointing regulatory genes involved in senescence might lead to tools that could effectively overcome this dilemma.

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“…Although this might be due to a combination of decreased synthesis plus enhanced degradation rates, the evidence shows clearly that rates of protein synthesis become negligible after complete leaf expansion (Makino et al, 1984; Mae, 2004), and expression of photosynthetic genes typically declines sharply in fully expanded, yet non-senescent leaves (e.g., Krupinska and Humbeck, 2004; Breeze et al, 2011). Chloroplast protein levels are mostly regulated by rates of degradation during senescence (Lamattina et al, 1985; Mae, 2004). An exception is the D1 protein, which is constantly subjected to proteolysis and resynthesis as part of a photodamage repair cycle (Aro et al, 1993; Guiamét et al, 2002); but in spite of its potential impact on photosynthetic rates, breakdown of D1 may not make a large contribution to N redistribution.…”

Section: Increased Degradation Not Reduced Rates Of Synthesis Drivementioning

confidence: 99%

Chloroplast Protein Degradation in Senescing Leaves: Proteases and Lytic Compartments

et al. 2019

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Leaf senescence is characterized by massive degradation of chloroplast proteins, yet the protease(s) involved is(are) not completely known. Increased expression and/or activities of serine, cysteine, aspartic, and metalloproteases were detected in senescing leaves, but these studies have not provided information on the identities of the proteases responsible for chloroplast protein breakdown. Silencing some senescence-associated proteases has delayed progression of senescence symptoms, yet it is still unclear if these proteases are directly involved in chloroplast protein breakdown. At least four cellular pathways involved in the traffic of chloroplast proteins for degradation outside the chloroplast have been described (i.e., “Rubisco-containing bodies,” “senescence-associated vacuoles,” “ATI1-plastid associated bodies,” and “CV-containing vesicles”), which differ in their dependence on the autophagic machinery, and the identity of the proteins transported and/or degraded. Finding out the proteases involved in, for example, the degradation of Rubisco, may require piling up mutations in several senescence-associated proteases. Alternatively, targeting a proteinaceous protein inhibitor to chloroplasts may allow the inhibitor to reach “Rubisco-containing bodies,” “senescence-associated vacuoles,” “ATI1-plastid associated bodies,” and “CV-containing vesicles” in essentially the way as chloroplast-targeted fluorescent proteins re-localize to these vesicular structures. This might help to reduce proteolytic activity, thereby reducing or slowing down plastid protein degradation during senescence.

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Protein Metabolism in Senescing Wheat Leaves

Cited by 25 publications

References 19 publications

Expression of Early Light-Inducible Proteins in Flag Leaves of Field-Grown Barley

Expression of Early Light-Inducible Proteins in Flag Leaves of Field-Grown Barley

Leaf senescence and nutrient remobilisation in barley and wheat

Chloroplast Protein Degradation in Senescing Leaves: Proteases and Lytic Compartments

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