The Signal Peptide Peptidase Is Required for Pollen Function in Arabidopsis

Han, Sungwon; Green, Laura; Schnell, Danny J.

doi:10.1104/pp.108.130252

Cited by 26 publications

(25 citation statements)

References 54 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Based on these results, it is conceivable that AtSPP is involved in regulating growth and differentiation in Arabidopsis . This notion is supported by a knockout of the AtSPP gene giving rise to a lethal phenotype [16]. However, the target molecule of SPP in plants remains unresolved.…”

Section: Introductionmentioning

confidence: 99%

Experimental detection of proteolytic activity in a signal peptide peptidase of Arabidopsis thaliana

et al. 2013

View full text Add to dashboard Cite

BackgroundSignal peptide peptidase (SPP) is a multi-transmembrane aspartic protease involved in intramembrane-regulated proteolysis (RIP). RIP proteases mediate various key life events by releasing bioactive peptides from the plane of the membrane region. We have previously isolated Arabidopsis SPP (AtSPP) and found that this protein is expressed in the ER. An AtSPP-knockout plant was found to be lethal because of abnormal pollen formation; however, there is negligible information describing the physiological function of AtSPP. In this study, we have investigated the proteolytic activity of AtSPP to define the function of SPPs in plants.ResultsWe found that an n-dodecyl-ß-maltoside (DDM)-solubilized membrane fraction from Arabidopsis cells digested the myc-Prolactin-PP-Flag peptide, a human SPP substrate, and this activity was inhibited by (Z-LL)2-ketone, an SPP-specific inhibitor. The proteolytic activities from the membrane fractions solubilized by other detergents were not inhibited by (Z-LL)2-ketone. To confirm the proteolytic activity of AtSPP, the protein was expressed as either a GFP fusion protein or solely AtSPP in yeast. SDS-PAGE analysis showed that migration of the fragments that were cleaved by AtSPP were identical in size to the fragments produced by human SPP using the same substrate. These membrane-expressed proteins digested the substrate in a manner similar to that in Arabidopsis cells.ConclusionsThe data from the in vitro cell-free assay indicated that the membrane fraction of both Arabidopsis cells and AtSPP recombinantly expressed in yeast actually possessed proteolytic activity for a human SPP substrate. We concluded that plant SPP possesses proteolytic activity and may be involved in RIP.

show abstract

Section: Introductionmentioning

confidence: 99%

Experimental detection of proteolytic activity in a signal peptide peptidase of Arabidopsis thaliana

et al. 2013

View full text Add to dashboard Cite

show abstract

“…Studies performed on spp heterozygotes indicate that the protein is involved in pollen development and germination (Hoshi et al 2013). The SPPL1, SPPL2 and SPPL3 transcripts were detected in the tissues, roots, rosette leaves, cauline leaves, stems, flower-bud clusters, siliques and dry seeds (Han et al 2009) The significant accumulation of all three transcripts was; however, observed during seed germination. The SPPL3 transcript accumulates additionally during seed stratification and under dark treatment in response to sucrose (Grennan 2006).…”

Section: Rhomboids In a Thalianamentioning

confidence: 99%

“…The interesting fact is that this effect was reversed by the expression of both active and inactive presenilin variants, suggesting that the protease acts independently from the c-secretase complex (Khandelwal et al 2007). SPP is a proteolytically active protein crucial for A. thaliana development, since knockout of the SPP gene resulted in a lethal phenotype (Han et al 2009, Hoshi et al 2013. Studies performed on spp heterozygotes indicate that the protein is involved in pollen development and germination (Hoshi et al 2013).…”

Section: Rhomboids In a Thalianamentioning

confidence: 99%

Arabidopsis thaliana intramembrane proteases

et al. 2017

View full text Add to dashboard Cite

Proteolysis is considered as a crucial factor determining the proper development of the plant and its efficient functioning in variable environmental conditions. The role of proteases in protein quality control and protein turnover processes is well documented. The results of studies performed in recent years reveal; however, that proteolytic enzymes also participate in signal transduction pathways by releasing membrane-anchored transcription factors in the process known as regulated intramembrane proteolysis (RIP). The first described intramembrane protease was identified in human cells in 1997. In turn, the first plant intramembrane protease was identified in 2005, in Arabidopsis thaliana. To date, most studies concerning the RIP process in plants have been performed on this model plant. The knowledge concerning the potential physiological role of RIP is very limited. However, continuously accumulating information concerning this issue indicates that RIP, like the other proteolytic mechanisms, has a significant effect on plant ontogenesis, acclimatization and fertility. The aim of this article is to gather and systemize the present knowledge concerning the intramembrane proteases in A. thaliana.

show abstract

“…It is a short (5-30 amino acids long) peptide present at the N-terminus of the majority of newly synthesized proteins that are destined towards the secretory pathway. The importance of Bioinformatic characterization of aspartic protease (AP) enzyme in seed plants signal peptide has been investigated in different studies and it has been proved that the signal peptide is required for pollen function in Arabidopsis thaliana (Han et al 2009). Transmembrane domains of representative plants were studied in topology prediction.…”

Section: Discussionmentioning

confidence: 99%

Bioinformatic characterization of aspartic protease (AP) enzyme in seed plants

Darabi

Seddigh

2015

Plant Syst Evol

View full text Add to dashboard Cite

Aspartic proteases (APs; EC: 3.4.23) are a catalytic type of protease enzymes that use an activated water molecule bound to one or more aspartate residues for catalysis of their peptide substrates. They have been extensively studied and are widely distributed among vertebrates, plants, yeast, nematodes, parasites, fungi, and viruses. In this study, bioinformatic analyses of AP enzyme were performed in seed plants protein sequences, including 33 species of 14 different families. According to the conserved motifs obtained by MEME and MAST tools, two motifs were common in all seed plants. The structural and functional analyses of six selected monocots and dicots were investigated by ProtParam, SOPMA, SignalP 4.1, TMHMM 2.0 and ProDom tools in ExPASy database. Tertiary structure of Arabidopsis thaliana as a sample of seed plants, was predicted by Phyre2 server using ''d1oewa'' model (PDB accession code: 1oew) and its quality was verified by PRO-CHECK and ProSA-web servers. The protein sequences were aligned with ClustalW algorithm by MEGA 6.06 software and phylogenetic tree was constructed using the Neighbor-joining (NJ) method. In protein-protein interactions analysis by STRING 9.1 tool, 12 and 135 significant protein interaction groups were identified in Arabidopsis thaliana and other species, respectively. According to the results, there is a high identity among APs of different species in seed plants, so that they should be derived from a common ancestor. The approaches and results reported here would be useful to prioritize candidate genes for further functional proteomic studies of this enzyme in seed plants.

show abstract

The Signal Peptide Peptidase Is Required for Pollen Function in Arabidopsis

Cited by 26 publications

References 54 publications

Experimental detection of proteolytic activity in a signal peptide peptidase of Arabidopsis thaliana

Experimental detection of proteolytic activity in a signal peptide peptidase of Arabidopsis thaliana

Arabidopsis thaliana intramembrane proteases

Bioinformatic characterization of aspartic protease (AP) enzyme in seed plants

Contact Info

Product

Resources

About