The phosphocreatine shuttle of sea urchin sperm: flagellar creatine kinase resulted from a gene triplication.

Wothe, Donald; Charbonneau, Harry; Shapiro, Bennett M.

doi:10.1073/pnas.87.13.5203

Cited by 73 publications

(39 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Possible cases include creatine kinase from sperm flagella of the sea urchin (Strongylocentrotus purpuratus), which is a M r 145 protein having three apparently homologous regions (15); these could be catalytic domains, but their individual activities were not determined. Also, the cDNA of a polysaccharide hydrolase encodes three multi-functional catalytic domains, each with three different enzymatic activities (16), but no sequence data were provided.…”

Section: Resultsmentioning

confidence: 99%

Three functional luciferase domains in a single polypeptide chain

Hong

Hastings

1997

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

We report a unique case of a gene containing three homologous and contiguous repeat sequences, each of which, after excision, cloning, and expression in Escherichia coli, is shown to code for a peptide catalyzing the same reaction as the native protein, Gonyaulax polyedra luciferase (M r ‫؍‬ 137). This enzyme, which catalyzes the light-emitting oxidation of a linear tetrapyrrole (dinof lagellate luciferin), exhibits no sequence similarities to other luciferases in databases. Sequence analysis also reveals an unusual evolutionary feature of this gene: synonymous substitutions are strongly constrained in the central regions of each of the repeated coding sequences.

show abstract

Section: Resultsmentioning

confidence: 99%

Three functional luciferase domains in a single polypeptide chain

Hong

Hastings

1997

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…Among them are several kinds of kinases (25)(26)(27)(28)(29) and polysaccharide-degrading enzymes such as chitinases (30)(31)(32), xylanases (33,34), and endoglucanases (35). Homology between the domains varies from Ϸ30% to 99%; activities of the individual domains have not been demonstrated in all cases, and pH and temperature optima, as well as substrate preference, have been reported to differ among the domains.…”

Section: Discussionmentioning

confidence: 99%

Molecular evolution of dinoflagellate luciferases, enzymes with three catalytic domains in a single polypeptide

Liu

Wilson

Hastings

2004

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Enzymes with multiple catalytic sites are rare, and their evolutionary significance remains to be established. This study of luciferases from seven dinoflagellate species examines the previously undescribed evolution of such proteins. All these enzymes have the same unique structure: three homologous domains, each with catalytic activity, preceded by an N-terminal region of unknown function. Both pairwise comparison and phylogenetic inference indicate that the similarity of the corresponding individual domains between species is greater than that between the three different domains of each polypeptide. Trees constructed from each of the three individual domains are congruent with the tree of the full-length coding sequence. Luciferase and ribosomal DNA trees both indicate that the Lingulodinium polyedrum luciferase diverged early from the other six. In all species, the amino acid sequence in the central regions of the three domains is strongly conserved, suggesting it as the catalytic site. Synonymous substitution rates also are greatly reduced in the central regions of two species but not in the other five. This lineage-specific difference in synonymous substitution rates in the central region of the domains correlates inversely with the content of GC 3, which can be accounted for by the biased usage toward C-ending codons at the degenerate sites. RNA modeling of the central region of the L. polyedrum luciferase domain suggests a function of the constrained synonymous substitutions in the circadian-controlled protein synthesis.codon bias ͉ domain duplication ͉ synonymous substitutions T he luciferase (LCF) of the bioluminescent dinoflagellate Lingulodinium polyedrum (Lp; formerly Gonyaulax polyedra) has three homologous tandemly arranged 377-aa-long domains, each of which is catalytically active (1). The LCF of another dinoflagellate, Pyrocystis lunula (Pl), has a similar structure (2). In both, we found the amino acids in the central region of each of the three domains to be highly conserved intramolecularly at Ϸ95% identity, compared with Ϸ65% in the flanking regions. Remarkably, and only in Lp, there were fewer synonymous substitutions in the central region.These results are intriguing from both evolutionary and mechanistic viewpoints. To grasp their significance, we investigated the LCFs of five other bioluminescent dinoflagellates, all of which are photosynthetic: Alexandrium affine (Aa), Alexandrium tamarense (At), Pyrocystis fusiformis (Pf ), Pyrocystis noctiluca (Pn), and Protoceratium reticulatum (Pr). All were shown to have the same basic configuration, i.e., tandem triplication of catalytic domains following an Ϸ110-aa-long N-terminal sequence. Fortuitously, it turned out that Lp and Pl LCFs represent extremes of a spectrum of LCF structures with regard to synonymous substitution rates in the central region of each domain.Bioluminescence in dinoflagellates has been well characterized only in Lp, where the three components involved in light emission are packaged together in unique cellular organelles,...

show abstract

“…Wothe et a/. (35) reported that S. purpuratus sperm tail creatine kinase contains three complete but not identical creatine kinase segments and that each segment has a high degree of sequence similarity to other mammalian creatine kinase. Therefore, we suppose that H. pulcherrimus sperm tail creatine kinase may also have similar segments.…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of Sperm Creatine Kinase and Guanylate Cyclase of the Sea Urchin Hemicentrotus pulcherrimus

1992

View full text Add to dashboard Cite

Creatine kinase and guanylate cyclase were purified from Hernicentrotus pulcherrirnus spermatozoa The molecular weight of the purified sperm tail creatine kinase was estimated to be 137,000 by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Sperm tail guanylate cyclase was purified by chromatography on a WGA-Sepharose column connected to a Concanavalin A-Sepharose column, and a Superose 12 HR column. The molecular weight of the tail guanylate cyclase was estimated to be 128,000 by SDS-PAGE. The specific activity of the purified enzyme was 8.25 pmol of cGMP formedlminimg protein. Sperm-activating peptide I (SAP-I) causes an electrophoretic mobility shift of H. pulcherrimus sperm guanylate cyclase from 131 kDa to 128 kDa. The 131 kDa form of guanylate cyclase was co-purified with a 76 kDa protein, whose molecular mass is similar to that of a SAP-I receptor. The purified 131 kDa form of guanylate cyclase had higher activity than the 128 kDa form. The 131 kDa and 128 kDa forms of guanylate cyclase contained 23.83k0.65 and 4.16k0.45 moles of phosphate per mol protein (mean+S.D. ; n=3), respectively. The activities of guanylate cyclase and creatine kinase increased during the testis development. During spermatogenesis, sperm tail creatine kinase was detected immunohistochemically only in mature spermatozoa.

show abstract

The phosphocreatine shuttle of sea urchin sperm: flagellar creatine kinase resulted from a gene triplication.

Cited by 73 publications

References 33 publications

Three functional luciferase domains in a single polypeptide chain

Three functional luciferase domains in a single polypeptide chain

Molecular evolution of dinoflagellate luciferases, enzymes with three catalytic domains in a single polypeptide

Purification and Characterization of Sperm Creatine Kinase and Guanylate Cyclase of the Sea Urchin Hemicentrotus pulcherrimus

Contact Info

Product

Resources

About