Structure and function of the receptor-like protein kinases of higher plants

Walker, John C.

doi:10.1007/bf00016492

Cited by 254 publications

(113 citation statements)

References 46 publications

(62 reference statements)

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“…Analysis of the predicted amino acid sequence showed that the encoded protein is a SERK member belonging to the LRR-RLK superfamily (Walker, 1994). All the domains characteristic of the SERK proteins reported in other plant species are present in CaSERK.…”

Section: Discussionmentioning

confidence: 99%

Isolation and Expression Analysis of a SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE (SERK) Gene in Curcuma alismatifolia Gagnep.

Sucharitakul¹,

Rakmit²,

Boonsorn³

et al. 2014

JAS

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Somatic embryogenesis provides a useful tool to facilitate efficient mass propagation in plants. The SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE (SERK) gene serves a fundamentally important role in somatic embryogenesis of many plant species. The isolation of a SERK gene homolog, namely CaSERK, from Curcuma alismatifolia Gagnep. cv. Blue Tung, was reported. Prediction of coding sequence showed that it encoded a protein of 628 amino acids showing high similarity to previously characterized SERK sequences and containing all the features shared by members of the SERK family, including five leucine-rich repeats and the distinctive proline-rich SPP domain. Investigation of CaSERK expression revealed that its transcripts were found throughout the whole somatic embryogenesis process with highest abundance in embryogenic callus. These results indicate that CaSERK might have somatic embryogenesis-associated functions in this economically important ornamental ginger. Detection of CaSERK transcript accumulation in flower and coma bract tissues is suggestive of its additional roles in other developmental signaling pathways.

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Section: Discussionmentioning

confidence: 99%

Isolation and Expression Analysis of a SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE (SERK) Gene in Curcuma alismatifolia Gagnep.

Sucharitakul¹,

Rakmit²,

Boonsorn³

et al. 2014

JAS

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“…Human AGT concentrations were measured both with the BCA dye binding assay (15) and spectrophotometrically using a molar extinction coefficient, ⑀ 280 ϭ 3.93 ϫ 10 4 M Ϫ1 cm Ϫ1 , calculated from data of Roy et al (16). The values of ⑀ 215 /⑀ 280 ϭ 8.2 and ⑀ 260 /⑀ 280 ϭ 0.63 were obtained from UV spectra of the purified protein dissolved in 10 mM Tris buffer (pH 7.6) at 21°C.…”

Section: Methodsmentioning

confidence: 99%

DNA-binding Mechanism ofO 6-Alkylguanine-DNA Alkyltransferase

Rasimas

Pegg

Fried³

2003

Journal of Biological Chemistry

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The mutagenic and cytotoxic effects of many endogenous and exogenous alkylating agents are mitigated by the actions of O 6 -alkylguanine-DNA alkyltransferase (AGT). In humans this protein protects the integrity of the genome, but it also contributes to the resistance of tumors to DNA-alkylating chemotherapeutic agents. Here we report properties of the interaction between AGT and short DNA oligonucleotides. We show that although AGT sediments as a monomer in the absence of DNA, it binds cooperatively to both single-stranded and double-stranded deoxyribonucleotides. This strong cooperative interaction is only slightly perturbed by active site mutation of AGT or by alkylation of either AGT or DNA. The stoichiometry of complex formation with 16-mer oligonucleotides, assessed by analytical ultracentrifugation and electrophoretic mobility shift assays, is 4:1 on single-stranded and duplex DNA and is unchanged by several active site mutations or by protein or DNA alkylation. These results have significant implications for the mechanisms by which AGT locates and interacts with repairable alkyl lesions to effect DNA repair. O6 -Alkylguanine-DNA alkyltransferase is a ubiquitous repair protein that plays a vital role in minimizing the mutagenic effects of alkylating agents (1-4). It catalyzes the stoichiometric transfer of a variety of alkyl substituents from the O 6 -position of guanine to an active site cysteine, preventing incorrect base pairing caused by these adducts. More than 100 alkyltransferases are now known, and the crystal structures are available for three family members: the Ada-C protein from Escherichia coli (5), the human alkyltransferase (hAGT) 1 (6), and the protein from the thermophilic archaeon, Pyrococcus kodakaraensis (7). All of the known alkyltransferases lack the ability to dealkylate themselves, and no dealkylation activity has been found in cell extracts to date. On this basis, it is widely thought that alkyltransferase participates in a single reaction and is then irreversibly inactivated. Given the apparently nonenzymatic nature of the protein, the protection afforded by alkyltransferase is likely to depend on the regulation of its synthesis and degradation and on its ability to efficiently locate repairable lesions throughout the genome.The mechanisms by which AGT interacts with adduct-containing and adduct-free DNAs are poorly understood. Two contrasting mechanisms have been proposed to date. In the first, single AGT proteins bind normal and lesion-containing DNA, and the distribution of AGT between normal and lesion sites depends on a difference in binding affinity. This model is consistent with the observation that a single AGT monomer is necessary and sufficient to dealkylate a single O 6 -alkyl guanine adduct within a DNA duplex (3). It is supported by the observation that single AGT-DNA complexes are detected by gel shift assay when AGT binds short DNA molecules. These complexes have been interpreted as having a 1:1 AGT:DNA stoichiometry, and the binding affinities have been calculated ...

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“…Plant RLKs are classified according to sequence motifs in the putative extracellular receptor domains (Hardie, 1999). One of the largest and best studied classes of RLKs is characterized by the Leu-rich repeat (LRR) known to be involved in protein-protein interaction (Walker, 1994). The second class includes the family of S-domain RLKs (SRKs) of Brassicaceae with high similarity to S-locus glycoproteins (SLGs) involved in the self-incompatibility response (Nasrallah et al, 1994).…”

mentioning

confidence: 99%

“…The second class includes the family of S-domain RLKs (SRKs) of Brassicaceae with high similarity to S-locus glycoproteins (SLGs) involved in the self-incompatibility response (Nasrallah et al, 1994). An S-domain contains a characteristic array of Cys residues and other conserved motifs (Walker, 1994). The third class, represented in Arabidopsis by LECRK1 and LRK1, contain a lectin-like extracellular domain that may bind oligosaccharides, such as the elcitors derived from breakdown of the cell wall (Herve et al, 1996).…”

mentioning

confidence: 99%