Identification of an Arabidopsis inorganic pyrophosphatase capable of being imported into chloroplasts

Schulze, Silke; Mant, Alexandra; Koßmann, Jens; Lloyd, J. R.

doi:10.1016/j.febslet.2004.03.080

Cited by 33 publications

(40 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Arabidopsis encodes six soluble inorganic PPases and three membrane-bound H + -translocating PPases (Schulze et al, 2004;Ferjani et al, 2011). The H + translocating PPases are located in the tonoplast or the Golgi apparatus, while the soluble PPases are located in the cytosol or chloroplast (AtPPa6; Schulze et al, 2004). None of these genes are up-regulated in senescing leaves like AtTTM1.…”

Section: Discussionmentioning

confidence: 99%

“…Removal of PP i prevents these reactions from reaching equilibrium and plays an important role in maintaining the direction of these reactions (Maeshima, 2000). Arabidopsis encodes six soluble inorganic PPases and three membrane-bound H + -translocating PPases (Schulze et al, 2004;Ferjani et al, 2011). The H + translocating PPases are located in the tonoplast or the Golgi apparatus, while the soluble PPases are located in the cytosol or chloroplast (AtPPa6; Schulze et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Triphosphate Tunnel Metalloenzyme Function in Senescence Highlights a Biological Diversification of This Protein Superfamily

et al. 2017

View full text Add to dashboard Cite

ORCID IDs: 0000-0003-3889-6183 (W.M.); 0000-0002-3797-4277 (K.Y.).The triphosphate tunnel metalloenzyme (TTM) superfamily comprises a group of enzymes that hydrolyze organophosphate substrates. They exist in all domains of life, yet the biological role of most family members is unclear. Arabidopsis (Arabidopsis thaliana) encodes three TTM genes. We have previously reported that AtTTM2 displays pyrophosphatase activity and is involved in pathogen resistance. Here, we report the biochemical activity and biological function of AtTTM1 and diversification of the biological roles between AtTTM1 and 2. Biochemical analyses revealed that AtTTM1 displays pyrophosphatase activity similar to AtTTM2, making them the only TTMs characterized so far to act on a diphosphate substrate. However, knockout mutant analysis showed that AtTTM1 is not involved in pathogen resistance but rather in leaf senescence. AtTTM1 is transcriptionally up-regulated during leaf senescence, and knockout mutants of AtTTM1 exhibit delayed dark-induced and natural senescence. The double mutant of AtTTM1 and AtTTM2 did not show synergistic effects, further indicating the diversification of their biological function. However, promoter swap analyses revealed that they functionally can complement each other, and confocal microscopy revealed that both proteins are tail-anchored proteins that localize to the mitochondrial outer membrane. Additionally, transient overexpression of either gene in Nicotiana benthamiana induced senescence-like cell death upon dark treatment. Taken together, we show that two TTMs display the same biochemical properties but distinct biological functions that are governed by their transcriptional regulation. Moreover, this work reveals a possible connection of immunity-related programmed cell death and senescence through novel mitochondrial tail-anchored proteins.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Triphosphate Tunnel Metalloenzyme Function in Senescence Highlights a Biological Diversification of This Protein Superfamily

et al. 2017

View full text Add to dashboard Cite

show abstract

“…PPa isoforms were confirmed in planta as described by Schulze et al (2004). In planta mean normalized expression levels of most of the PPa isoforms were quite low (data not shown).…”

Section: Response To Different Carbohydrate Sources In Plantamentioning

confidence: 74%

“…has six sPPase isoforms (Schulze et al, 2004;Öztürk et al, 2014). The presence of a vacuolar membrane localized proton-pumping PPase (Geingenberger et al, 1998;Farre et al, 2001) and data implying the importance of a large cytosolic PP i pool for plant growth and development (Jelitto et al, 1992;Sonnewald, 1992) suggested lack of cytosolic sPPase activity.…”

Section: Discussionmentioning

confidence: 99%

“…genome has six sPPase isoforms, one of which was shown to be localized in the plastids and the others in the cytosol and/or nucleus (Schulze et al, 2004;George et al, 2010;Öztürk et al, 2014). Navarro-De la Sancha et al (2007) reported the possibility of ubiquitous expression of A. thaliana sPPase isoforms based on the GENEVESTIGATOR database and suggested that changes in cytosolic PP i concentration by differential expression of sPPase isoforms might be important in the regulation of plant metabolism (NavarroDe la Sancha et al, 2007;Meyer et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Differential expression of soluble pyrophosphatase isoforms inArabidopsis upon external stimuli

Öztürk

Greiner²,

Rausch³

2015

Turk J Bot

View full text Add to dashboard Cite

In plants, pyrophosphate (PP i ), generated in a wide range of reversible anabolic reactions, is hydrolyzed by pyrophosphatases. The presence of tonoplast-and Golgi-integral H + -translocating pyrophosphatases in plants led to the conclusion that plant cytosol has no soluble pyrophosphatase activity. However, the Arabidopsis thaliana (L.) Heynh. genome also encodes five soluble pyrophosphatase isoforms (PPas). There are almost no data in the literature on their redundancy in plant metabolism; therefore, we performed expression analyses of A. thaliana soluble pyrophosphatase isoforms in response to external stimuli including carbohydrate status, hormone action, and stress exposure. The results revealed pronounced specificity for each isoform. Interestingly, one isoform (PPa3; At2g46860) was specifically induced during seedling etiolation, and in the presence of the nonmetabolizable sugar 3-O-methylglucose. Based on quantitative PCR analyses, PPa1 (At1g01050) and PPa4 (At3g53620) appeared to be regulated by sugars. Quantitative PCR analyses indicated isoform-and tissue-dependent responses of PPa isoforms to ABA, salt, and cold stresses. PPa2 (At2g18230) and PPa5 (At4g01480) responded differentially to salinity, cold treatment, and ABA. We conclude that plant cytosolic pyrophosphatases perform multiple, so far overlooked functions during plant development and stress exposure.

show abstract

A comparative proteome and phosphoproteome analysis of differentially regulated proteins during fertilization in the self‐incompatible species Solanum chacoense Bitt.

et al. 2007

View full text Add to dashboard Cite

We have used 2-DE for a time-course study of the changes in protein and phosphoprotein expression that occur immediately after fertilization in Solanum chacoense. The phosphorylation status of the detected proteins was determined with three methods: in vivo labeling, immunodetection, and phosphoprotein-specific staining. Using a pI range of 4-7, 262 phosphorylated proteins could be mapped to the 619 proteins detected by Sypro Ruby staining, representing 42% of the total proteins. Among these phosphoproteins, antibodies detected 184 proteins from which 78 were also detected with either of the other two methods (42%). Pro-Q Diamond phosphoprotein stain detected 111 proteins, of which 76 were also detected with either of the other two methods (68%). The 32P in vivo labeling method detected 90 spots from which 78 were also detected with either of other two methods (87%). On comparing before and after fertilization profiles, 38 proteins and phosphoproteins presented a reproducible change in their accumulation profiles. Among these, 24 spots were selected and analyzed by LC-MS/MS using a hybrid quadrupole-TOF (Q-TOF) instrument. Peptide data were searched against publicly available protein and EST databases, and the putative roles of the identified proteins in early fertilization events are discussed.

show abstract

Identification of an Arabidopsis inorganic pyrophosphatase capable of being imported into chloroplasts

Cited by 33 publications

References 29 publications

Triphosphate Tunnel Metalloenzyme Function in Senescence Highlights a Biological Diversification of This Protein Superfamily

Triphosphate Tunnel Metalloenzyme Function in Senescence Highlights a Biological Diversification of This Protein Superfamily

Differential expression of soluble pyrophosphatase isoforms inArabidopsis upon external stimuli

A comparative proteome and phosphoproteome analysis of differentially regulated proteins during fertilization in the self‐incompatible species Solanum chacoense Bitt.

Contact Info

Product

Resources

About