The human rod photoreceptor cGMP phosphodiesterase β‐subunit

Khramtsov, N.V.; Feshchenko, Elena A; Suslova, Veronika A.; Shmukler, Boris E.; Terpugov, B.E.; Rakitina, Tatiana V.; Atabekova, N. V.; Липкин, В. М.

doi:10.1016/0014-5793(93)81003-i

Cited by 21 publications

(12 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The region near the N terminus of CyaB1 protein is similar to the N-terminal regions of the cyclic GMP (cGMP)-stimulated cGMP phosphodiesterases. This region of CyaB1, which contains 270 amino acids, shows 21.6% identity to the bovine cGMP-stimulated phosphodiesterase (44), 19.3% identity to the bovine cGMP-binding, cGMP-specific phosphodiesterase (32), and 16.7% identity to the beta subunit of the human photoreceptor cGMP phosphodiesterase (27). In mammals, this region is proposed to be an allosteric cGMP-binding region of phosphodiesterases (32).…”

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

View full text Add to dashboard Cite

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...

show abstract

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

View full text Add to dashboard Cite

show abstract

“…Thus, human cone PDEcd amino acid sequence deduced from the cDNA structure consists of 858 residues with calculated molecular mass of 99169 Da. Human cone PDE~' has 89.1% and 82.7% homology to bovine [6] and chicken [13] cone PDEa', respectively; 63.8% homology to human rod PDE a subunit [14]; and 64.5% homology to human rod PDE 13 subunit [7]. Human cone PDEct', like mammalian visual PDEs, has an internal homologous repeat of the amino acid sequence in its N-terminal part.…”

Section: Ass ~A~h~aaatatatat T Gctag~ C Caaaaatc C Cac Ggc~ataaagt mentioning

confidence: 99%

“…The last 4 residues at the C-terminus conform to the CAAX consensus motif for multistep posttranslational processing covering lipidation, proteolysis and carboxymethylation [15]. Sequence analysis of genomic clones and comparison of the structure obtained with the corresponding sequences of bovine cone PDEct' cDNA [6] and human rod PDE [3-subunit gene [7] indicated the presence of fourteen N-terminal exons and 5'-flanking region. Table 1 presents data available on the exon/intron organization of this 5' part of human PDEa' gene.…”

Section: Ass ~A~h~aaatatatat T Gctag~ C Caaaaatc C Cac Ggc~ataaagt mentioning

confidence: 99%

See 1 more Smart Citation

Human cone‐specific cGMP phosphodiesterase α′ subunit: Complete cDNA sequence and gene arrangement

et al. 1996

View full text Add to dashboard Cite

Four independent phage clones containing the fragments of cone-specific cGMP phosphodiesterase (PDE) c~' subunit (PDEc() cDNA were isolated from the human cDNA library. The screening of the genomic library resulted in isolation of four independent phage clones with the fragments of human cone PDEo~' gene including 5'-flanking region and exons ranged from 1 to 14 (overall 32 kilobases). Structural studies of the clones made it possible to establish the complete human cone PDEc( cDNA structure (3455 base pairs). The encoding polypeptide consists of 858 amino acid residues with a calculated molecular mass of 99169 Da. The deduced amino acid sequence displays high homology to the earlier analyzed catalytic cq [3 and c~' subunits of bovine, human, chicken and mouse photoreceptor PDEs.

show abstract

“…1,2A, Beavo 1995, McAllisterLucas et a/. 1993, Khramtsov et a/. 1993, Anabaena -adenylate cyclases, and the f. coli transcription factor EhlA .…”

mentioning

confidence: 99%

Biochemical Characterization of an Adenylate Cyclase, CyaB1, in the Cyanobacterium Anabaena sp. Strain PCC 7120

2001

View full text Add to dashboard Cite

The cyanobacterial cyaBl gene encodes a novel type of adenylate cyclase. The catalytic domain is located in the carboxyl-terminal half, while the GAF and PAS domains are conserved in the amino-terminal half. Recombinant CyaBl and a truncated CyaBl lacking the amino-terminal domain (AN-CyaBl) were purified and characterized. The purified CyaBl is activated by divalent cations, such as Mg2+ and Mn2+, like other types of adenylate cyclase. The activity of CyaBl was slightly elevated by forskolin, but was not affected by cGMP, irrespective of the presence of the cGMP binding motif in the GAF domain. The specific activity of AN-CyaBl is one-eighteenth that of CyaB1, whereas the Km values of both proteins are almost the same. The results suggest that the amino-terminal half has a positive regulatory effect on the catalytic activity.

show abstract

The human rod photoreceptor cGMP phosphodiesterase β‐subunit

Cited by 21 publications

References 18 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

Human cone‐specific cGMP phosphodiesterase α′ subunit: Complete cDNA sequence and gene arrangement

Biochemical Characterization of an Adenylate Cyclase, CyaB1, in the Cyanobacterium Anabaena sp. Strain PCC 7120

Contact Info

Product

Resources

About