Purification of Calreticulin-like Protein(s) from Spinach Leaves

Menegazzi, Pamela; Guzzo, Flavia; Baldan, Barbara; Mariani, Paolina; Treves, Susan

doi:10.1006/bbrc.1993.1167

Cited by 64 publications

(44 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In animals, the protein has demonstrated many regulatory functions, such as protein processing, inner cellular Ca 2+ balance regulation, cell adhesion and control of expression of steroid-sensitive genes and apoptosis. Calreticulin genes were initially isolated from barley (Chen et al, 1994) and spinach (Menegazzi et al, 1993), additional calreticulin cDNA sequences were subsequently cloned from tobacco (Denecke et al, 1993), corn (Kwiatkowski et al, 1995, Dresselhaus et al, 1996, Chinese cabbage (Beassica pekinensis) (Lim et al, 1996), Arabidopsis (Nelson et al, 1997), rice (Li and Komatsu, 2000), pea (Pisum sativum) and Ginkgo biloba.…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning of a new wheat calreticulin gene TaCRT1 and expression analysis in plant defense responses and abiotic stress resistance

An¹,

Lin²,

FengTao³

et al. 2011

Genet. Mol. Res.

View full text Add to dashboard Cite

ABSTRACT. Calreticulin proteins play essential roles in regulating various metabolic processes and in molecular signal transduction in animals and plants. Using homologous PCR, we screened a cDNA library of the wheat resistance gene Yr5 from a near-isogenic line in the susceptible common wheat variety Taichung 29, which was inoculated with an incompatible race CYR32 of Puccinia striiformis. We isolated a novel full-length cDNA encoding calreticulin protein, which we named TaCRT1. Sequence analyses indicated that TaCRT1 contains an open reading frame of 1287 bp in length; it was deduced to encode 428 amino acids. Clustering analysis showed that TaCRT1 belongs to group III of the calreticulin protein family. Semi-quantitative RT-PCR was used to analyze expression profiles of the isolated gene under biotic and abiotic stresses. Expression of TaCRT1 was suppressed by exogenous application of phytohormones, such as abscisic acid and methyl jasmonate, and by dehydration; but it was induced by CYR32 infection and cold treatment. Based on the expression patterns, ©FUNPEC-RP www.funpecrp.com.br Genetics and Molecular Research 10 (4): 3576-3585 (2011) TaCRT1 in plant defense and stress resistance in wheat 3577we propose that TaCRT1 participates in regulatory processes involved in defense responses and stress resistance in wheat.

show abstract

Section: Introductionmentioning

confidence: 99%

Molecular cloning of a new wheat calreticulin gene TaCRT1 and expression analysis in plant defense responses and abiotic stress resistance

An¹,

Lin²,

FengTao³

et al. 2011

Genet. Mol. Res.

View full text Add to dashboard Cite

show abstract

“…CRT has been purified from leaves (Menegazzi et al, 1993), and Crt cDNAs have been found during searches for proteins associated with pollination (Chen et al, 1994), for proteins containing ER-retention signals (Denecke et al, 1995), for glycosylated proteins (Benedetti and Turner, 1995), and by immunological screening (Kwiatkowski et al, 1995).…”

mentioning

confidence: 99%

Abundant Accumulation of the Calcium-Binding Molecular Chaperone Calreticulin in Specific Floral Tissues of Arabidopsis thaliana

1997

View full text Add to dashboard Cite

Calreticulin (CRT) is a calcium-binding protein in the endoplasmic reticulum (ER) with an established role as a molecular chaperone. An additional function in signal transduction, specifically in calcium distribution, is suggested but not proven. We have analyzed the expression pattern of Arabidopsis thaliana CRTs for a comparison with these proposed roles. Three CRT genes were expressed, with identities of the encoded proteins ranging from 54 to 86%. Protein motifs with established functions found in CRTs of other species were conserved. CRT was found in all of the cells in low amounts, whereas three distinct floral tissues showed abundant expression: secreting nectaries, ovules early in development, and a set of subepidermal cells near the abaxial surface of the anther. Localization in the developing endosperm, which is characterized by high protein synthesis rates, can be reconciled with a specific chaperone function. Equally, nectar production and secretion, a developmental stage marked by abundant ER, may require abundant CRT to accommodate the traffic of secretory proteins through the ER. Localization of CRT in the anthers, which are degenerating at the time of maximum expression of CRT, cannot easily be reconciled with a chaperone function but may indicate a role for CRT in anther maturation or dehiscence.

show abstract

“…"CS-like proteins" were also described in Pistia stratiotes (Franceschi et al, 1993) and in red beet and cucumber cells (Xing et al, 1994). In contrast, Menegazzi et al (1993), Denecke et al (1993Denecke et al ( , 1995, and Hassan et al (1995), investigating the identity of Ca2+-binding proteins in spinach leaves, tobacco seedlings, and pea seeds, respectively, found sequence homologies with animal CR. Chen et al (1994) reported the identification of cDNA clones encoding CR in barley.…”

mentioning

confidence: 99%

“…Along this line, we have undertaken a deeper biochemical characterization of the Ca2+-binding proteins previously identified by some of us (Menegazzi et al, 1993) in spinach leaves. Here we provide conclusive evidence that CR, and not CS, is expressed in spinach leaves.…”

mentioning

confidence: 99%