Literature DB >> 8589932

The sequence and expression of the gamma-VPE gene, one member of a family of three genes for vacuolar processing enzymes in Arabidopsis thaliana.

T Kinoshita1, M Nishimura, I Hara-Nishimura.   

Abstract

Vacuolar processing enzymes (VPEs) are responsible for the maturation of seed proteins. Southern blot analysis showed that a family of genes for VPEs in Arabidopsis thaliana was composed of three genes, for alpha-VPE, beta-VPE and gamma-VPE, respectively. The gene for gamma-VPE was isolated from a genomic library. It was composed of nine exons and eight introns. The positions of the introns were fully conserved among the three genes, with the exception that the alpha-VPE gene was missing the fifth intron found in the beta-VPE and gamma-VPE genes. The predicted gamma-VPE protein was 80% and 57% identical in terms of amino acid sequence to the alpha-VPE protein and beta-VPE protein, respectively. Northern blot analysis demonstrated that the gamma-VPE gene was expressed predominantly in the stems, with a lower level of expression in rosette and cauline leaves. However, the expression was not detected in roots, flowers plus buds, or green siliques, in contrast to the high-level expression of the beta-VPE gene in the flowers plus buds. Thus, gamma-VPE seems to be an isoform that is specific to vegetative organs. Members of the VPE family can be separated into two subfamilies, one that is specific to seeds and another that is specific to vegetative organs, such as leaves and stems. The members of the seed subfamily might function in the protein-storage vacuoles of seeds, while those of the vegetable subfamily might function in the lytic vacuoles of non-storage organs.

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Year:  1995        PMID: 8589932

Source DB:  PubMed          Journal:  Plant Cell Physiol        ISSN: 0032-0781            Impact factor:   4.927


  19 in total

1.  A slow maturation of a cysteine protease with a granulin domain in the vacuoles of senescing Arabidopsis leaves.

Authors:  K Yamada; R Matsushima; M Nishimura; I Hara-Nishimura
Journal:  Plant Physiol       Date:  2001-12       Impact factor: 8.340

2.  Redundant proteolytic mechanisms process seed storage proteins in the absence of seed-type members of the vacuolar processing enzyme family of cysteine proteases.

Authors:  Darren Fred Gruis; David A Selinger; Jill M Curran; Rudolf Jung
Journal:  Plant Cell       Date:  2002-11       Impact factor: 11.277

3.  Storage protein accumulation in the absence of the vacuolar processing enzyme family of cysteine proteases.

Authors:  Darren Gruis; Jan Schulze; Rudolf Jung
Journal:  Plant Cell       Date:  2003-12-19       Impact factor: 11.277

4.  Storage reserve accumulation in Arabidopsis: metabolic and developmental control of seed filling.

Authors:  Sébastien Baud; Bertrand Dubreucq; Martine Miquel; Christine Rochat; Loïc Lepiniec
Journal:  Arabidopsis Book       Date:  2008-07-24

5.  A vacuolar processing enzyme, deltaVPE, is involved in seed coat formation at the early stage of seed development.

Authors:  Satoru Nakaune; Kenji Yamada; Maki Kondo; Tomohiko Kato; Satoshi Tabata; Mikio Nishimura; Ikuko Hara-Nishimura
Journal:  Plant Cell       Date:  2005-02-10       Impact factor: 11.277

Review 6.  A cut above the rest: the regulatory function of plant proteases.

Authors:  Andreas Schaller
Journal:  Planta       Date:  2004-10-29       Impact factor: 4.116

7.  Identification, cDNA cloning and possible roles of seed-specific rice asparaginyl endopeptidase, REP-2.

Authors:  Hideki Kato; Keita Sutoh; Takao Minamikawa
Journal:  Planta       Date:  2003-04-09       Impact factor: 4.116

8.  Molecular cloning and characterization of Vigna mungo processing enzyme 1 (VmPE-1), an asparaginyl endopeptidase possibly involved in post-translational processing of a vacuolar cysteine endopeptidase (SH-EP).

Authors:  T Okamoto; T Minamikawa
Journal:  Plant Mol Biol       Date:  1999-01       Impact factor: 4.076

9.  Diverse range of gene activity during Arabidopsis thaliana leaf senescence includes pathogen-independent induction of defense-related genes.

Authors:  B F Quirino; J Normanly; R M Amasino
Journal:  Plant Mol Biol       Date:  1999-05       Impact factor: 4.076

10.  Nucellain, a barley homolog of the dicot vacuolar-processing protease, is localized in nucellar cell walls.

Authors:  C Linnestad; D N Doan; R C Brown; B E Lemmon; D J Meyer; R Jung; O A Olsen
Journal:  Plant Physiol       Date:  1998-12       Impact factor: 8.340

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