Plant-specific insertions in the soybean aspartic proteinases, soyAP1 and soyAP2, perform different functions of vacuolar targeting

Terauchi, Kaede; Asakura, Tomiko; Ueda, Haruko; Tamura, Tomoko; Tamura, Kentaro; Matsumoto, Ichiro; Misaka, Takumi; Hara‐Nishimura, Ikuko; Abe, Keiko

doi:10.1016/j.jplph.2005.08.007

Cited by 33 publications

(30 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Its presence does not appear to be essential for the maintenance of AP enzymatic activity (Asakura et al 2000;Tormakangas et al 2001), however, some data point to a possible role for the PSI in the correct vacuolar sorting of some plant APs (Mutlu and Gal 1999;Tormakangas et al 2001;Simões and Faro 2004). This is the case for barley phytepsin and for the soybean aspartic proteinase soyAP2, but not for soyAP1 in which deletion of the PSI has no eVect on the vacuolar targeting (Terauchi et al 2006). …”

Section: Discussionmentioning

confidence: 99%

Processing and trafficking of a single isoform of the aspartic proteinase cardosin A on the vacuolar pathway

Duarte

Pissarra

Moore

2008

Planta

View full text Add to dashboard Cite

Cardosin A is the major vacuolar aspartic proteinase (APs) (E.C.3.4.23) in pistils of Cynara cardunculus L. (cardoon). Plant APs carry a unique domain, the plant-specific-insert (PSI), and a pro-segment which are separated from the catalytic domains during maturation but the sequence and location of processing steps for cardosins have not been established. Here transient expression in tobacco and inducible expression in Arabidopsis indicate that processing of cardosin A is conserved in heterologous species. Pulse chase analysis in tobacco protoplasts indicated that cleavage at the carboxy-terminus of the PSI could generate a short-lived 50 kDa intermediate which was converted to a more stable 35 kDa intermediate by removal of the PSI. Processing intermediates detected immunologically in tobacco leaves and Arabidopsis seedlings confirmed that cleavage at the amino-terminus of the PSI either preceded or followed quickly after cleavage at its carboxy-terminus. Thus removal of PSI preceded the loss of the prosegment in contrast to the well-characterised barley AP, phytepsin. PreprocardosinA acquired a complex glycan and its processing was inhibited by brefeldin A and dominant-inhibitory AtSAR1 or AtRAB-D2(a )mutants indicating that it was transported via the Golgi and that processing followed ER export. The 35 kDa intermediate was present in the cell wall and protoplast culture medium as well as the vacuole but the 31 kDa mature subunit, lacking the amino-terminal prosegment, was detected only in the vacuole. Thus maturation appears to occur only after sorting from the trans-Golgi to the vacuole. Processing or transport of cardosin A was apparently slower in tobacco protoplasts than in whole cells.

show abstract

Section: Discussionmentioning

confidence: 99%

Processing and trafficking of a single isoform of the aspartic proteinase cardosin A on the vacuolar pathway

Duarte

Pissarra

Moore

2008

Planta

View full text Add to dashboard Cite

show abstract

“…The physiological, structural and functional relevance of this domain is unknown (Guevara et al, 2002). It is thought that the PSI is not critical for enzymatic 0031 (Asakura et al, 2000), however, roles such as protein targeting to the vacuole, proper folding, vesicle leakage, and structure-function have been identified (Tormakangas et al, 2001;Egas et al, 2000;Payie et al, 2003;Simoes and Faro, 2004;Terauchi et al, 2006). The PSI was found to undergo proteolytic cleavage resulting in its partial or total removal during activation of the enzyme to produce a single-chain or a two-chain mature form or a complex mixture of products Simoes and Faro, 2004).…”

Section: Introductionmentioning

confidence: 99%

Structure–function characterization of the recombinant aspartic proteinase A1 from Arabidopsis thaliana

et al. 2010

View full text Add to dashboard Cite

“…Recombinant wheat and moss phytepsins in which the PSI had been removed failed to be sorted to the vacuole (Tormakangas et al, 2001;Schaaf et al, 2004), which further supports the vacuoletargeting role of the PSI. However, Terauchi et al (2006) have demonstrated that the PSI in SoyAP1 is not involved in vacuole targeting, since PSI-deleted SoyAP1 was still targeted to the vacuole. The authors concluded that the vacuolar targeting functions of the PSI depend on the AP type.…”

Section: Resultsmentioning

confidence: 96%

An aspartic acid protease from common bean is expressed ‘on call’ during water stress and early recovery

Contour-Ansel

Torres-Franklin

Zuily-Fodil

et al. 2010

Journal of Plant Physiology

View full text Add to dashboard Cite

Plant-specific insertions in the soybean aspartic proteinases, soyAP1 and soyAP2, perform different functions of vacuolar targeting

Cited by 33 publications

References 34 publications

Processing and trafficking of a single isoform of the aspartic proteinase cardosin A on the vacuolar pathway

Processing and trafficking of a single isoform of the aspartic proteinase cardosin A on the vacuolar pathway

Structure–function characterization of the recombinant aspartic proteinase A1 from Arabidopsis thaliana

An aspartic acid protease from common bean is expressed ‘on call’ during water stress and early recovery

Contact Info

Product

Resources

About