Changes in chloroplast FtsH-like gene during cold acclimation in alfalfa (Medicago sativa)

Ivashuta, Sergey; Imai, Ryozo; Uchiyama, Kazuhiro; Gau, Mitsuru; Shimamoto, Yuta

doi:10.1078/0176-1617-00661

Cited by 19 publications

(17 citation statements)

References 30 publications

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“…17). FtsH represents an ATP‐dependent temperature‐sensitive metalloprotease in plant chloroplasts and bacteria, indicating that proteolytic activity may play an important role in plastid functionality during stress adaptation 22, 23. As reported formerly 24 the FtsH gene from Bacillus subtilis displays sensitivity to salt stress.…”

Section: Resultsmentioning

confidence: 87%

Short‐term effects of salt exposure on the maize chloroplast protein pattern

et al. 2009

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It is of fundamental importance to understand the physiological differences leading to salt resistance and to get access to the molecular mechanisms underlying this physiological response. The aim of this work was to investigate the effects of short-term salt exposure on the proteome of maize chloroplasts in the initial phase of salt stress (up to 4 h). It could be shown that sodium ions accumulate quickly and excessively in chloroplasts in the initial phase of moderate salt stress. A change in the chloroplast protein pattern was observed without a change in water potential of the leaves. 2-DE revealed that 12 salt-responsive chloroplast proteins increased while eight chloroplast proteins decreased. Some of the maize chloroplast proteins such as CF1e and a Ca(2+)-sensing receptor show a rather transient response for the first 4 h of salt exposure. The enhanced abundance of the ferredoxin NADPH reductase, the 23 kDa polypeptide of the photosystem II, and the FtsH-like protein might reflect mechanism to attenuate the detrimental effects of Na(+) on the photosynthetic machinery. The observed transient increase and subsequent decrease of selected proteins may exhibit a counterbalancing effect of target proteins in this context. Intriguingly, several subunits of the CF1-CF0 complex are unequally affected, whereas others do not respond at all.

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Section: Resultsmentioning

confidence: 87%

Short‐term effects of salt exposure on the maize chloroplast protein pattern

et al. 2009

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“…Spot 10 in leaves and spot 11 in roots were identified as filamentation temperature-sensitive H (FtsH) 2B and their levels were up-regulated under salt stress, FtsH, an ATP and Zn 2+ -dependent protein, has the activities of ATPase, protease and molecular chaperone (Langer, 2000). Previous studies have shown that the levels of FtsH-like protein were up-regulated in leaf chloroplasts under salt stress (Zörb et al, 2009), and it was closely related to abiotic stress (Ivashuta et al, 2002). However, their exact functions in salt tolerance are not known.…”

Section: Classification Of Salt Responsive Proteinsmentioning

confidence: 98%

Salt stress induced proteome and transcriptome changes in sugar beet monosomic addition line M14

Yang

Wang

et al. 2012

Journal of Plant Physiology

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“…It should be noted that increased FtsH transcript level in response to high light was observed also in alfalfa seedlings and Synechocystis sp. PCC 6803 (Huang et al 2002, Ivashuta et al 2002).…”

Section: Introductionmentioning

confidence: 99%

FtsH proteases in chloroplasts and cyanobacteria

Adam

Zaltsman

Sinvany-Villalobo

et al. 2004

Physiologia Plantarum

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FtsH is a membrane‐bound ATP‐dependent metalloprotease complex found in prokaryotes and organelles of eukaryotic cells. It consists of one or two trans‐membrane helices at its amino‐terminus, a highly conserved ATPase domain, which relates it to the AAA protein family, and a zinc‐binding domain towards its carboxy‐terminus that serves as the proteolytic site. Most bacteria contain a single FtsH gene, but the cyanobacterium Synechocystis has four. The Arabidopsis thaliana genome contains 12 genes encoding FtsH proteins, nine of them can be targeted to chloroplasts, whereas the other three are mitochondrial. Chloroplast FtsH protease is located in the thylakoid membrane, where it forms complexes, most likely hexamers, whose ATPase and proteolytic domains are exposed to the stroma. It is involved in the degradation of the D1 protein of photosystem II reaction centre during its repair from photoinhibition, as well as in the degradation of unassembled proteins in the thylakoid and the stroma. In Arabidopsis, FtsH2 is the most abundant isomer, followed by FtsH5, 8 and 1. This hierarchy is well reflected in the severity of the variegated phenotype of mutants in these genes.

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Changes in chloroplast FtsH-like gene during cold acclimation in alfalfa (Medicago sativa)

Cited by 19 publications

References 30 publications

Short‐term effects of salt exposure on the maize chloroplast protein pattern

Short‐term effects of salt exposure on the maize chloroplast protein pattern

Salt stress induced proteome and transcriptome changes in sugar beet monosomic addition line M14

FtsH proteases in chloroplasts and cyanobacteria

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