Stress proteins co-expressed in suberized and lignified cells and in apical meristems

Pla, María; Huguet, Gemma; Verdaguer, Dolors; Puigderrajols, Pere; Llompart, Blanca; Nadal, Anna; Molinas, Marisa

doi:10.1016/s0168-9452(98)00169-1

Cited by 49 publications

(34 citation statements)

References 45 publications

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“…The abundance of P450 monooxygenases and of oxidases reflects the high complexity of synthesizing the cork polymeric matrix and indicates that cork cell metabolism must generate reactive oxygen species in high amounts. This corresponds to previous observations showing that cork cells suffer from fairly high oxidative stress (Pla et al, 1998(Pla et al, , 2000. Here, we found that ascorbate peroxidase, a crucial enzyme for H 2 O 2 detoxifying in plant cells (Davletova et al, 2005), was strongly up-regulated in cork.…”

Section: Linkages Between Aliphatic and Aromatic Unitssupporting

confidence: 92%

A Genomic Approach to Suberin Biosynthesis and Cork Differentiation

Soler

Serra²,

Molinas³

et al. 2007

Plant Physiology

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141

139

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Cork (phellem) is a multilayered dead tissue protecting plant mature stems and roots and plant healing tissues from water loss and injuries. Cork cells are made impervious by the deposition of suberin onto cell walls. Although suberin deposition and cork formation are essential for survival of land plants, molecular studies have rarely been conducted on this tissue. Here, we address this question by combining suppression subtractive hybridization together with cDNA microarrays, using as a model the external bark of the cork tree (Quercus suber), from which bottle cork is obtained. A suppression subtractive hybridization library from cork tree bark was prepared containing 236 independent sequences; 69% showed significant homology to database sequences and they corresponded to 135 unique genes. Out of these genes, 43.5% were classified as the main pathways needed for cork biosynthesis. Furthermore, 19% could be related to regulatory functions. To identify genes more specifically required for suberin biosynthesis, cork expressed sequence tags were printed on a microarray and subsequently used to compare cork (phellem) to a non-suberin-producing tissue such as wood (xylem). Based on the results, a list of candidate genes relevant for cork was obtained. This list includes genes for the synthesis, transport, and polymerization of suberin monomers such as components of the fatty acid elongase complexes, ATP-binding cassette transporters, and acyltransferases, among others. Moreover, a number of regulatory genes induced in cork have been identified, including MYB, No-Apical-Meristem, and WRKY transcription factors with putative functions in meristem identity and cork differentiation.

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Section: Linkages Between Aliphatic and Aromatic Unitssupporting

confidence: 92%

A Genomic Approach to Suberin Biosynthesis and Cork Differentiation

Soler

Serra²,

Molinas³

et al. 2007

Plant Physiology

Self Cite

141

139

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“…The QsHsp10.4-CI coding region was excised from the phage clone kgt11-QsHsp10.4-CI by EcoRI digestion, blunt-ending and BsmFI digestion. Then it was cloned in the vector resulting from BsmI digestion, blunt-ending and BsmFI digestion of pBluescriptHsp17.4 (Pla et al 1998). This intermediate plasmid was digested with EcoRI and XhoI and the insert was subsequently cloned into the pET29a expression vector, previously digested with the same restriction enzymes.…”

Section: Cloning Of Hsp-cismentioning

confidence: 99%

“…130 lg of protein was loaded in each gel. In both oneand two-dimensional (2D) electrophoresis, proteins were transferred onto polyvinylidenedifluoride (PVDF) membranes (Millipore) and incubated with polyclonal antibody raised against recombinant QsHsp17.4-CI protein in rabbit (Pla et al 1998). Bound antibodies were detected using peroxidase-conjugated goat anti-rabbit IgG (GAR-Po; Nordic Immunology) and a chemiluminescence system (BM Chemiluminescence Western Blotting Substrate; Boehringer Mannheim).…”

Section: Electrophoresis and Immunological Detection Of Proteinsmentioning

confidence: 99%

“…Living cork cells were obtained from phellem (outer bark of cork oak trees). For the assays, two oligonucleotides were used designed in highly conserved regions near the 5¢ and 3¢ ends of the previously cloned cork oak Qshsp17.4-CI (Pla et al 1998; Fig. 1).…”

Section: Shsp-cis In Cork Tissuementioning

confidence: 99%

“…10-kDa sHsp-CIs in oxidatively stressed tissues To investigate the possible accumulation in cork cells of highly truncated sHsps, we performed 2D immunoassays using a polyclonal antibody anti-Hsp17.4-CI (Pla et al 1998). For this purpose, cork (phellem) and wood tissue, which are both under high endogenous oxidative stress conditions were analysed together with stem tissue of plantlets growing in standard conditions and subjected to heat (42°C, 3 h) or to oxidative stress (5% H 2 O 2 , 5 h; Fig.…”

Section: Shsp-cis In Cork Tissuementioning

confidence: 99%

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A 10-kDa class-CI sHsp protects E. coli from oxidative and high-temperature stress

Jofré

Molinas

Pla

2003

Planta

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We report on a new cDNA clone (Qshsp10.4-CI) of a Quercus suber L. class-CI small heat-shock protein (sHsp) obtained from cork (phellem), a highly oxidatively stressed plant tissue. The deduced gene product lacks the C-terminal extension and the consensus I region of the alpha-crystallin domain, being the most C-terminally truncated sHsp reported to date. In an attempt to prove that a protective function is possible for such a truncated sHsp, we overexpressed in Escherichia coli three recombinant sHsp-CIs, one (rQsHsp10.4-CI) showing the same truncation as Qshsp10.4-CI, a second (rN49) lacking the whole alpha-crystallin domain, and a third (rN153) consisting of a full-length sHsp-CI. The overexpression of rN153 and, remarkably, rQsHsp10.4-CI but not rN49 enhanced cell viability under high temperature and, interestingly, under oxidative stress. These results show that the C-terminal extension and the consensus I region of the alpha-crystallin domain are dispensable, but amino acids 1-41 of the alpha-crystallin domain (including the consensus II region) are essential for the protective activity of sHsp-CIs. On the other hand, two-dimensional immunodetection patterns showed accumulation of ca. 10-kDa sHsp-CI immunorelated polypeptides in cork and other oxidatively stressed tissues but not in control and heat-stressed tissues. We discuss the possible role of highly truncated sHsps in relation to oxidative stress.

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The Holm Oak leaf proteome: Analytical and biological variability in the protein expression level assessed by 2‐DE and protein identification tandem mass spectrometry de novo sequencing and sequence similarity searching

Jorge

Navarro

Lenz³

et al. 2005

Proteomics

104

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As a first approach in establishing the holm oak leaf proteome, we have optimised a protocol for this plant and tissue which includes the following steps: trichloroacetic acid-acetone extraction, two-dimensional gel electrophoresis (2-DE) on pH 5 to 8 linear gradient immobilised pH gradient strips as the first dimension, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis on 13% polyacrylamide gels as the second one. Proteins were detected by Coomassie staining. Gel images were recorded and digitalized, and the protein spots quantified by using a linear regression equation of protein quantity on spot volume obtained against standard proteins. Analytical variance was calculated for one-hundred protein spots from three replicate 2-DE gels of the same protein extract. Biological variance was determined for the same protein spots from independent tissue extracts corresponding to leaves from different trees, or the same tree at different orientations or sampling times during a day. Values of 26% for the analytical variance and 58.6% for the biological variance among independent trees were obtained. These values provide a quantified and statistical basis for the evaluation of protein expression changes in comparative proteomic investigations with this species. A representative set of the major proteins, covering the isoelectric point range of 5 to 8 and the relative molecular mass(r) range of 14 to 78 kDa, were subjected to liquid chromatography-tandem mass spectrometry analysis. Due to the absence of Quercus DNA or protein sequence databases, a method based on the procedure reported by Liska and Shevchenko including de novo sequencing and BLAST similarity searching against other plant species databases was used for protein identification. Out of 43 analysed spots, 35 were positively identified. The identified proteins mainly corresponded to enzymes involved in photosynthesis and energetic metabolism, with a significant number corresponding to RubisCO.

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Stress proteins co-expressed in suberized and lignified cells and in apical meristems

Cited by 49 publications

References 45 publications

A Genomic Approach to Suberin Biosynthesis and Cork Differentiation

A Genomic Approach to Suberin Biosynthesis and Cork Differentiation

A 10-kDa class-CI sHsp protects E. coli from oxidative and high-temperature stress

The Holm Oak leaf proteome: Analytical and biological variability in the protein expression level assessed by 2‐DE and protein identification tandem mass spectrometry de novo sequencing and sequence similarity searching

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