Interaction of a Protein Phosphatase with an
            <i>Arabidopsis</i>
            Serine-Threonine Receptor Kinase

Stone, Julie M.; Collinge, Margaret A.; Smith, Robert; Horn, Mark A.; Walker, John C.

doi:10.1126/science.7973632

Cited by 268 publications

(235 citation statements)

References 34 publications

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“…This domain was found in several unrelated proteins, as well as in some transcription factors and kinases, and is supposed to be involved in a nuclear signaling. This region of CyaD shows 41.4% identity to the FHA domain of human antigen KI-67, which is thought to be required for maintaining cell proliferation (41), and 38.6% identity to the FHA domain of kinaseassociated protein phosphatase of Arabidopsis thaliana (46).…”

Section: Resultsmentioning

confidence: 99%

Isolation and characterization of multiple adenylate cyclase genes from the cyanobacterium Anabaena sp. strain PCC 7120

Katayama

Ohmori

1997

J Bacteriol

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Adenylate cyclase genes, designated cyaA, cyaB1, cyaB2, cyaC, and cyaD, were isolated from the filamentous cyanobacterium Anabaena sp. strain PCC 7120 by complementation of a strain of Escherichia coli defective for the presence of cya. These genes encoded polypeptides consisting of 735, 859, 860, 1,155, and 546 amino acid residues, respectively. Deduced amino acid sequences of the regions near the C-terminal ends of these cya genes were similar to those of catalytic domains of eukaryotic adenylate cyclases. The remaining part of each cya gene towards its N-terminal end showed a characteristic structure. CyaA had two putative membrane-spanning regions. Both CyaB1 and CyaB2 had regions that were very similar to the cyclic GMP (cGMP)-binding domain of cGMP-stimulated cGMP phosphodiesterase. CyaC consisted of four distinct domains forming sequentially from the N terminus: a response regulator-like domain, a histidine kinase-like domain, a response regulatorlike domain, and the catalytic domain of adenylate cyclase. CyaD contained the forkhead-associated domain in its N-terminal region. Expression of these genes was examined by reverse transcription-PCR. The transcript of cyaC was shown to be predominant in this cyanobacterium. The cellular cyclic AMP level in the disruptant of the cyaC mutant was much lower than that in the wild type.Cyclic AMP (cAMP) regulates various biological activities in both prokaryotes and eukaryotes. In prokaryotes, cAMP and cAMP receptor protein regulate gene expression (7). In eukaryotes, cAMP regulates enzyme activity (11), channel activity (42), and gene expression (34) via the cAMP-dependent protein kinase. In cyanobacteria, it has been reported that cellular cAMP content is affected by growth conditions (17,22), that cAMP concentration changes rapidly in response to light-off and light-on signals (37) or to a pH shift (36), and that cAMP interferes with the pattern formation of heterocysts (43). However, it is still unknown whether cAMP functions as an intracellular signal molecule in cyanobacteria.Recently, we isolated adenylate cyclase (cya) genes from the filamentous cyanobacteria Anabaena cylindrica (26) and Spirulina platensis (52). Regions near the C-terminal ends of the adenylate cyclases of both cyanobacteria showed significant structural similarity to the catalytic domain of the adenylate cyclase of eukaryotes but showed no homology to that of prokaryotes such as Escherichia coli. Furthermore, cyanobacterial adenylate cyclases appeared to be membrane oriented.To study the physiological functions of these adenylate cyclases, disruption or overexpression of cya genes is indispensable. Unfortunately, both A. cylindrica and S. platensis are not transformable, so they are not suitable for this purpose. In this study, we isolated cya genes from a transformable cyanobacterium, Anabaena sp. strain PCC 7120, and constructed mutants defective in cya genes. Some physiological properties of these mutants were determined. MATERIALS AND METHODSStrains and growth conditions. Anabaena sp. s...

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Section: Resultsmentioning

confidence: 99%

Isolation and characterization of multiple adenylate cyclase genes from the cyanobacterium Anabaena sp. strain PCC 7120

Katayama

Ohmori

1997

J Bacteriol

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“…A variety of molecular genetic and biochemical approaches have been employed with plant receptor-like kinases in an attempt to identify putative in vivo binding partners, including yeast two-hybrid analysis (Bower et al, 1996;Gu et al, 1998), interaction cloning (Stone et al, 1994;Braun et al, 1997), and immunoprecipitation and purification of receptor-protein complexes (Trotochaud et al, 1999). In addition to these methods, synthetic peptides have been extensively used in animal Tyr receptor kinase research to understand binding motifs and KD substrate recognition consensus sequences (for review, see Kuriyan and Cowburn, 1997).…”

Section: Discussionmentioning

confidence: 99%

“…However, the KDs of numerous plant receptor-like kinases have been expressed as recombinant proteins in Escherichia coli and they do indeed behave as functional kinases in vitro (Braun and Walker, 1996;SchulzeMuth et al, 1996;Wang et al, 1996;Braun et al, 1997;Williams et al, 1997;Muschietti et al, 1998;Stone et al, 1998;Coello et al, 1999;van der Knaap et al, 1999). Moreover, the recombinant KDs have been used as molecular probes for interaction cloning (Stone et al, 1994;Braun et al, 1997) and yeast twohybrid screens (Bower et al, 1996;Gu et al, 1998) have been used to identify intracellular substrates for plant receptor-like kinases. Phosphoamino acid analyses reveal that plant receptor-like kinases autophosphorylate on Ser and Thr residues (as opposed to Tyr in most animal receptor kinases), but a thorough analysis of specific autophosphorylation sites using biophysical techniques such as matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) has not yet been reported.…”

mentioning

confidence: 99%

Recombinant Brassinosteroid Insensitive 1 Receptor-Like Kinase Autophosphorylates on Serine and Threonine Residues and Phosphorylates a Conserved Peptide Motif in Vitro

Oh¹,

Ray²,

et al. 2000

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BRASSINOSTEROID-INSENSITIVE 1 (BRI1) encodes a putative Leucine-rich repeat receptor kinase in Arabidopsis that has been shown by genetic and molecular analysis to be a critical component of brassinosteroid signal transduction. In this study we examined some of the biochemical properties of the BRI1 kinase domain (BRI1-KD) in vitro, which might be important predictors of in vivo function. Recombinant BRI1-KD autophosphorylated on serine (Ser) and threonine (Thr) residues with p-Ser predominating. Matrix-assisted laser desorption/ionization mass spectrometry identified a minimum of 12 sites of autophosphorylation in the cytoplasmic domain of BRI1, including five in the juxtamembrane region (N-terminal to the catalytic KD), five in the KD (one each in sub-domains I and VIa and three in sub-domain VIII), and two in the carboxy terminal region. Five of the sites were uniquely identified (Ser-838, Thr-842, Thr-846, Ser-858, and Thr-872), whereas seven were localized on short peptides but remain ambiguous due to multiple Ser and/or Thr residues within these peptides. The inability of an active BRI1-KD to transphosphorylate an inactive mutant KD suggests that the mechanism of autophosphorylation is intramolecular. It is interesting that recombinant BRI1-KD was also found to phosphorylate certain synthetic peptides in vitro. To identify possible structural elements required for substrate recognition by BRI1-KD, a series of synthetic peptides were evaluated, indicating that optimum phosphorylation of the peptide required R or K residues at P Ϫ 3, P Ϫ 4, and P ϩ 5 (relative to the phosphorylated Ser at P ϭ 0).

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“…The family of proteins containing FHA domains, which includes proteins of diverse functional roles, is growing rapidly. Examples of the FHA family include: Dun1 and Rad53 (or Spk1), which are involved in DNA damage repair and the S phase checkpoint in Saccharomyces cerevisiae (Allen et al, 1994;Navas et al, 1995;Sun et al, 1998;Zheng et al, 1993); Cds1, the Schizosaccharomyces pombe homolog of Rad53 (Murakami & Okayama, 1995); Mek1, which is related to meitotic recombination of yeast (Leem & Ogawa, 1992); KAPP, kinase-associated protein phosphatase from Arobidopsis thaliana, which binds to the receptorlike protein kinase RLK5 (Stone et al, 1994); and Ki-67, a human nuclear protein related to cell proliferation (Schluter et al, 1993). The two most recent members are HuCds1 (or Chk2) in humans (Brown et al, 1999;Matsuoka et al, 1998), and Dmnk in Drosophila melanogaster (Oishi et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Structure and function of a new phosphopeptide-binding domain containing the FHA2 of rad53

Liao

Byeon

Tsai

1999

Journal of Molecular Biology

109

120

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Interaction of a Protein Phosphatase with an Arabidopsis Serine-Threonine Receptor Kinase

Cited by 268 publications

References 34 publications

Isolation and characterization of multiple adenylate cyclase genes from the cyanobacterium Anabaena sp. strain PCC 7120

Isolation and characterization of multiple adenylate cyclase genes from the cyanobacterium Anabaena sp. strain PCC 7120

Recombinant Brassinosteroid Insensitive 1 Receptor-Like Kinase Autophosphorylates on Serine and Threonine Residues and Phosphorylates a Conserved Peptide Motif in Vitro

Structure and function of a new phosphopeptide-binding domain containing the FHA2 of rad53

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