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PubMed1979

Structure-function studies on red pigment-concentrating hormone, II. The significance of the C-terminal tryptophan amide.

The significance of the C-terminal tryptophan residue of the red pigment-concentrating hormone (RPCH: Glu-Leu-Asn-Phe-Ser-Pro-Gly-Trp-NH2) regulating the blanching of the crustacean chromatophores has been investigated. RPCH and a number of analogues that differ only in the C-terminal part of the hormone, have been synthesized and assayed for biological activity on the shrimp Leander adspersus. It has been shown that the indole skeleton of tryptophan is an absolute requirement for the biological activity of the hormone. To provide maximum response the tryptophan must be blocked as the amide. The activity of synthetic [Tyr4]RPCH and adipokinetic hormone (AKH) purified from Schistocerca gregaria has been compared with the activity of synthetic RPCH.

Amides↗
PubMed1983

N-terminal sequences of subunits L and M of the photosynthetic reaction centre from Rhodospirillum rubrum G-9+. Separation of the subunits by gel filtration on hydroxypropylated Sephadex G 100 in organic solvents.

A new method has been developed by which subunits L and M of the photosynthetic reaction centre from Rhodospirillum rubrum G-9+ can be obtained in pure form, starting form freeze-dried chromatophore membranes. The method employs extraction into a mixture of chloroform/methanol and gel permeation chromatography on a column of hydroxypropylated Sephadex G 100. Cross-contamination of the purified subunits was less than 5% (mol/mol), as estimated by manual Edman degradation. Automated Edman degradation has been carried out with both subunits in a liquid-phase sequencer. 36 amino-acid residues of subunit L and 50 residues of subunit M could be unequivocally identified. In both cases, the sequence analyses came to a premature end as the signal sudden by dropped to the level of the accidental fluctuations of the phenylthiohydantoin-derivatives background. This effect is explained by the unusual susceptibility to peptide bond cleavage of certain threonine residues which probably underwent N leads to O acyl shift during the cleavage reactions. The N-terminal sequences have been compared to those of subunits L and M of the photosynthetic reactions centre from Rhodopseudomonas sphaeroides R-26 (sutton, M.R., Rosen, D., Feher, G. & Steiner, L.A. (1982) Biochemistry 21, 3842-3849). The homology among subunits L is close to 90% and thus markedly higher than that among subunits M (32%). This finding indicates a pre-eminent role of subunit L in the primary events of photosynthetic energy conversion.

Amino Acid Sequence↗
PubMed1986

Kinetic characterization and partial purification of the membrane-bound inorganic pyrophosphatase from Rhodopseudomonas palustris.

A membrane-bound inorganic pyrophosphatase from Rhodopseudomonas palustris has been studied by kinetic analysis. The enzymatic activity was stimulated by Mg2+, and the (Mg-PPi) complex is regarded to be the functional substrate. Free Mg2+ revealed a significant influence on the membrane-bound PPiase activity. Kinetic data were determined at various fixed concentrations of free Mg2+. Mg2+ is proposed to act as an activator in two ways. It may interact with the enzyme directly, and may combine with PPi to yield the functional substrate Mg-PPi. Ca2+ revealed a non-competitive type of inhibition on the Mg2+-activated enzyme. The membrane-bound PPiase activity was firmly attached to the chromatophore membrane. To achieve an almost entire solubilization, both, Triton X-100 and high concentrations of Mg2+, had to be applied. An enrichment method along with stepwise lowering the concentrations of Triton X-100 and Mg2+ after the solubilization has been established. The solubilized and partially purified enzyme was stimulated by phospholipids while the influence of free Mg2+ was lost. Three different energies of activation as a function of temperature were derived from Arrhenius plots for the membrane-bound as well as for the solubilized PPiase activity.

Calcium↗
PubMedDate not supplied

Respiratory electron flow and ATPase system in photosynthetically grown Rhodopseudomonas palustris.

Rhodopseudomonas palustris is grown photosynthetically on thiosulfate. As pointed out earlier, the chromatophore deficient cell-free fraction S-144,000 catalyzes the thiosulfate-linked ATP-dependent reversal of electron transfer in anaerobiosis, thus providing reducing equivalents in the form of NADH. Under aerobic conditions, this fraction also catalyzes the oxidation of NADH, ferro-cytochrome c, or ascorbate. ATP, ADP, and PPi are active in retarding the aerobic electron flow. The electron retardation is stimulated by the addition of Mg2+ due to a Mg2+-stimulated ATPase present. The ATPase system in S-144,000 hydrolyzes ATP, ADP, and PPi. Similarly, ATP or ADP, or even PPi can function as energy sources in order to achieve the reduction of pyridine nucleotide. The ATPase turnover is diminished by NADH or NAD+. Admixture of ascorbate results in an increased ATPase activity. Exactly the enhanced amount of adenine nucleotide hydrolysis caused by the addition of ascorbate is inhibited by cyanide.

Adenine Nucleotides↗
PubMed1998

The general kinetic model of electron transfer in photosynthetic reaction centers activated by multiple flashes.

A new general kinetic model for the functioning of photosynthetic reaction centers (RC) of purple bacteria, under multiple flash activation, has been developed. The model includes the primary electron donor (P870) as well as the primary (QA) and secondary (QB) acceptor quinones. The new features of this general model include: (1) consideration of four different states of the QB binding site (vacant, occupied by QB, by QB- and by QBH2), (2) incorporation of the dark relaxation of the RC between flashes, (3) the assumption of fast exchange of quinones between the RC and quinone pool in detergent micelles or chromatophore membrane, (4) description of the kinetics of electron transfer in both oxidized (no donor for P870+) and reduced (in the presence of donor for P870+) conditions simultaneously, (5) the consideration of both single and multiple flash activation of the RC of purple bacteria and (6) consideration of the cumulative effects of all previous flashes of the series in the response induced by the current flash. This model is used to calculate and predict (1) flash-induced binary oscillations of the secondary acceptor semiquinone (QB-), (2) flash-induced behavior of P870+ in the presence and absence of electron donor and (3) the apparent equilibrium constant of electron transfer between QA and QB and others. Different characteristics of RC are analyzed as a function of flash intensity, time between flashes, concentration of electron donor, redox-potential of the medium, concentration of pool quinone and quinol, association and dissociation equilibrium constants for quinone and quinol at the QB binding site, equilibrium constants of electron transfer between QA- and QB and between QA- and QB-, as well as the rate constants of oxidation of QA- and QB- by redox mediators. The proposed model can be used as a basis for assays of kinetic behavior of native and mutant RC of purple bacteria and for determination of the factors influencing the release of QH2 from RC. The latter is needed for analysis of factors controlling light-activated electron transport in the cytochrome bc1 complexes of purple bacteria by quinol molecules released from RC. The developed general approach for parallel consideration of flash-induced transitions of RC and its following dark relaxation between flashes can also be used for kinetic description of photosynthetic RC of oxygenic photosynthesis.

Electron Transport↗
PubMed2000

Heterodimeric versus homodimeric structure of the primary electron donor in Rhodobacter sphaeroides reaction centers genetically modified at position M202.

Using light-induced Fourier-transform infrared (FTIR) difference spectroscopy of the photo-oxidation of the primary donor (P) in chromatophores from Rhodobacter sphaeroides, we examined a series of site-directed mutants with His M202 changed to Gly, Ser, Cys, Asn or Glu in order to assess the ability of these side chains to ligate the Mg atom of one of the two bacteriochlorophylls (BChl) constituting P. In the P+QA-/PQA FTIR difference spectra of the mutants HG(M202), HS(M202), HC(M202) and HN(M202), the presence of a specific electronic transition at approximately 2650-2750 cm-1 as well as of associated vibrational (phase-phonon) bands at approximately 1560, 1480 and 1290 cm-1 demonstrate that these mutants contain a BChl/BChl homodimer like that in native reaction centers with the charge on P+ shared between the two coupled BChl. In contrast, the absence of all of these bands in HE(M202) shows that this mutant contains a BChl/bacteriopheophytin heterodimer with the charge localized on the single BChl, as previously determined for the mutant HL(M202). Furthermore, the spectra of the heterodimers HE(M202) and HL(M202) are very similar in the 4000-1200 cm-1 IR range. Perturbations of the 10a-ester and 9-keto carbonyl modes for both the P and P+ states are observed in the homodimer mutants reflecting slight variations in the conformation and/or in position of P. These perturbations are likely to be due to a repositioning of the dimer in the new protein cavity generated by the mutation.

Dimerization↗
PubMed2004

Differential toxicity of copper, zinc, and lead during the embryonic development of Chasmagnathus granulatus (Brachyura, Varunidae).

Ovigerous females of the estuarine crab Chasmagnathus granulatus were exposed to copper (0.01 and 1 mg/L), zinc (0.05, 1, and 10 mg/L), or lead (0.01 and 1 mg/L) during early, late, or whole embryonic development. None of the assayed heavy metals produced a significant mortality of females, neither a decrease in the number of hatched larvae nor a decrease in the egg incubation time, but several morphological abnormalities were detected in hatched larvae. The abnormalities were classified in three categories: eye, body pigmentary, and body morphological abnormalities. Those larvae with eye and body pigmentary abnormalities, particularly those involving retinal pigments and chromatophores, showed the highest incidence by exposure to the assayed metals. In addition, embryos were more susceptible to copper and zinc during the late period of development, whereas the effect of lead was greater during the early period of embryogenesis. Some teratogenic effects observed in C. granulatus embryos exposed to heavy metals, particularly the hypertrophy and hypopigmentation of eyes observed in the laboratory at a lead concentration as low as that reported for the natural environment, could be considered as sensitive biomarkers for this kind of pollutant.

Animals↗
PubMed2006

Isolation and characterization of two pigment-dispersing hormones from the whiteleg shrimp, Litopenaeus vannamei.

In crustaceans, the pigment-dispersing hormone (PDH) is released from the X-organ/sinus gland complex located in the eyestalks, and controls pigment dispersion in the chromatophores. Knowledge concerning the structure and activity of PDH in penaeid shrimps is remains limited, since natural PDH has been purified from only the Kuruma prawn, Marsupenaeus japonicus. In this study, two PDHs (Liv-PDH-A and -B) were purified from the sinus gland extracts of another penaeid species, the whiteleg shrimp, Litopenaeus vannamei, by two steps of reversed-phase HPLC, and their amino acid sequences were determined. They both consist of 18 amino acid residues, with a free N-terminus and an amidated C-terminus, the sequences of Liv-PDH-A and -B being NSELINSLLGIPKVMNDAamide and NSELINSLLGLPKVMNDAamide, respectively. These sequences are identical to those of mature PDHs deduced from cDNAs encoding L. vannamei PDH precursors cloned previously by other workers. Liv-PDH-A and -B showed significant pigment-dispersing activity in melanophores by in vivo bioassay.

Amino Acid Sequence↗
PubMed1978

Separation and partial purification of central nervous system peptides from Limulus polyphemus with hyperglycemic and chromatophorotropic activity in crustaceans.

1. Crude extracts of Limulus CNS cause hyperglycemia in Orconectes immunis and expand chromatophores in Uca pugilator. 2. The hyperglycemic action is due to a previously unknown polypeptide (LHGF) with an estimated molecular weight of 6400 daltons. LHGF is inactivated by hydrogen peroxide, pepsin, and protease, but unaffected by trypsin and brief boiling.3. The chromatophorotropic activity is due to the previously reported substance, LUC. LUC is shown to be a peptide with an approximate molecular weight of 1850 daltons; it is inactivated by hydrogen peroxide, protease, pepsin, trypsin, chymotrypsin, and thermolysin. 4. LUC and LHGF activity can be readily separated by gel filtration on a Sephadex G-25 column. 5. The similarity of LUC and LHGF to known crustacean hormones is dicussed.

Animals↗
PubMed1999

An ethogram of body patterning behavior in the biomedically and commercially valuable squid Loligo pealei off Cape Cod, Massachusetts.

Squids have a wide repertoire of body patterns; these patterns contain visual signals assembled from a highly diverse inventory of chromatic, postural, and locomotor components. The chromatic components reflect the activity of dermal chromatophore organs that, like the postural and locomotor muscles, are controlled directly from the central nervous system. Because a thorough knowledge of body patterns is fundamental to an understanding of squid behavior, we have compiled and described an ethogram (a catalog of body patterns and associated behaviors) for Loligo pealei. Observations of this species were made over a period of three years (> or = 440 h) and under a variety of behavioral circumstances. The natural behavior of the squid was filmed on spawning grounds off Cape Cod (northwestern Atlantic), and behavioral trials in the laboratory were run in large tanks. The body pattern components--34 chromatic (including 4 polarization components), 5 postural, and 12 locomotor--are each described in detail. Eleven of the most common body patterns are also described. Four of them are chronic, or long-lasting, patterns for crypsis; an example is Banded Bottom Sitting, which produces disruptive coloration against the substrate. The remaining seven patterns are acute; they are mostly used in intraspecific communication among spawning squids. Two of these acute patterns--Lateral Display and Mate Guarding Pattern--are used during agonistic bouts and mate guarding; they are visually bright and conspicuous, which may subject the squids to predation; but we hypothesize that schooling and diurnal activity may offset the disadvantage presented by increased visibility to predators. The rapid changeability and the diversity of body patterns used for crypsis and communication are discussed in the context of the behavioral ecology of this species.

Animal Communication↗
PubMed2002

Morphometric analysis of male reproductive features of octopodids (Mollusca: Cephalopoda).

Taxonomic accounts of octopodids frequently describe the spermatophore, the penis that releases the spermatophore from the internal organs, and the ligula and calamus that transfer it to a female. To explore relationships among these male features and body size, this study applies principal components analysis to data from 43 species of the family Octopodidae, or benthic octopuses. Covariation in penis and mantle length opposed by covariation in ligula and calamus lengths forms primary shape variation. Secondary shape variation is due to opposing variation between ligula and calamus lengths. Primary shape variation is greatest among shallow-water species. The calami and ligulae of diurnal and crepuscular shallow-water species are short compared to those of nocturnal shallow-water species. Because these structures contain heterogeneous collagen arrays and lack camouflaging chromatophore organs, they are white. Diurnal and crepuscular octopus species may minimize their lengths due to selection imposed by visual predators. Secondary shape variation is greater in deep-sea and high-latitude octopuses. Members of Voss's Eledoninae (except Eledone) and Graneledoninae and two species of Benthoctopus have exceptionally long calami and comparatively short ligulae; these lengths vary among members of the Bathypolypodinae. Variation in spermatophore length is independent of the structures considered.

Animals↗
PubMed2006

Signaling to the enemy? Body pattern expression and its response to external cues during hunting in the cuttlefish Sepia officinalis (Cephalopoda).

Cuttlefish can rapidly alter their appearance by using neurally controlled chromatophore organs. This ability may provide a window into their cognitive capacity. We test whether the changes in body pattern that occur during hunting depend on context. If they do, then it may be possible to use these changes to study cephalopod cognition while the animal is engaged in ecologically relevant tasks. We found consistent individual differences in the tendency of cuttlefish to hunt with the first two arms raised. We also found that cuttlefish usually darken their skin after they seize a prey item. This darkening is observed regardless of the identity of the prey (fish, crab, or shrimp), prey context (buried in sand, in a bare tank, or on top of a rock pile), or the presence of a sudden stimulus. The sudden stimulus was created by presenting an overhead model bird to the cuttlefish. The model induced components of the Deimatic Display, which is a form of antipredator behavior, suggesting that the model was perceived as a potential threat. Passing Cloud displays and the Darkening of the arms were significantly reduced after exposure to the model bird. The effect of a potential predator on body pattern expression during hunting suggests it may be possible to use these changes as a sensitive indicator of ecologically relevant learning.

Animal Communication↗
PubMed1997

Seasonal rhythm of red pigment concentrating hormone in the crayfish.

The content of red pigment concentrating hormone (RPCH) in the eye-stalk of the crayfish Procambarus clarkii varies seasonally, with maximum values during the summer months and the lowest values in winter. The responsiveness of tegumentary chromatophores to synthetic RPCH varies concurrently.

Animals↗
PubMedDate not supplied

Binding sites for melanin-concentrating hormone (MCH) in brain synaptosomes and membranes from peripheral tissues identified with highly tritiated MCH.

Melanin-concentrating hormone (MCH) is a neuropeptide occurring in the brain of all vertebrate species. In chromatophores of teleost fishes it induces pigment granule aggregation. In mammals, however, its physiological function is not yet clear. Attempts to identify the site(s) of its action by binding analysis failed because radioiodinated MCH with the natural sequence was devoid of biological activity. We have now synthesized an analogue of rat/human MCH, [Pra4,8,12,19]-MCH, containing four L-propargylglycine (Pra) residues in positions 4, 8, 12, and 19 for catalytic tritiation to norvaline ([3H4]Nva) residues, each of which containing four tritium atoms. The resulting [3H]-MCH ([(3H4)Nva4,8,12,19]-MCH) had a specific radioactivity of approx. 12,200 GBq/mmol (330 Ci/mmol) and retained a biological activity of 10% as compared to rat/human MCH when tested in the carp scale assay. A series of qualitative binding studies performed with rat crude membranes from brain and peripheal tissues as well as with rat brain synaptosomes using the [3H]-MCH radioligand provided the first evidence for the presence of MCH receptors in mammalian tissues. The data showed that specific binding is present in the hypothalamus, hippocampus and in the adrenal gland while none was detected in the brain cortex or spleen. Owing to the tendency of [3H]-MCH to non-specific binding to tissue, glass and plastic surfaces, a saturation binding analysis with this radioligand was not possible.

Amino Acid Sequence↗
PubMed2000

Slowing of proton transport processes in the structure of bacterial reaction centers and bacteriorhodopsin in the presence of dipyridamole.

Dipyridamole, 2,6-bis(diethanolamino)-4,8-dipiperidinopyrimido(5, 4-d)pyrimidine, is employed in clinical practice as a vasodilator. It can also inhibit a specific membrane protein (glycoprotein P) which pumps anticancer drugs out of tumor cells. Dipyridamole (10-4 M) markedly slows down the kinetics of the electrogenic phase of the photoelectric response in Rhodobacter sphaeroides chromatophores. This phase is due to proton transfer from the external medium to the secondary quinone acceptor in the reaction center. In purple membranes of bacterium Halobacterium salinarium containing bacteriorhodopsin dipyridamole (in its charged state) significantly slowed the kinetics of proton transfer from the primary donor, Asp-96 (in membranes from bacteria of wild type), or from the external medium (in D96N mutant) to the Schiff base. It is suggested that dipyridamole can influence the structural-dynamic state of membrane proteins including modification of the structure of their hydrogen bonds involved in proton-transport processes.

Bacteriorhodopsins↗
PubMed2001

Acute toxicity of (chloro-)catechols and (chloro-)catechol-copper combinations in Escherichia coli corresponds to their membrane toxicity in vitro.

(Chloro-)catechols are toxic for bacteria and higher organisms, but the mode of action is not yet clearly understood. We have compared the acute toxicity of different chlorinated catechols to Escherichia coli with membrane toxic effects, namely narcosis and uncoupling that we have determined in an in vitro assay. In vitro membrane toxicity was quantified by measuring the accelerated decay of the membrane potential of chromatophores isolated from Rhodobacter sphaeroides. Both acute and membrane toxicity increased with increasing degree of chlorination. Analysis of dose-response curves, pH dependence, and estimated membrane concentrations gave a consistent picture of the mechanisms of membrane toxicity: At pH 7, the higher-chlorinated catechols acted as uncouplers of oxidative and photophosphorylation, and the lower-chlorinated catechols and catechol acted as narcotics. In the case of 3,5-dichlorocatechol and 4-monochlorocatechol at pH 8.8, both mechanisms appeared to contribute to the overall toxicity. Copper exhibited a diverging effect on the toxicity of catechols and of (chloro-)catechols to E. coli. Whereas the presence of copper increased the toxicity of catechol and 4-monochlorocatechol, the toxicity of 3,5-dichlorocatechol, 3,4,5-trichlorocatechol, and tetrachlorocatechol decreased. Again, the results obtained with in vitro assays agreed with the acute toxicity observed in E. coli: The presence of copper accelerated decay of the membrane potential of catechol and 4-monochlorocatechol; however, the effect was reversed by copper in experiments with 3,5-dichlorocatechol, 3,4,5-trichlorocatechol, and tetrachlorocatechol. We have proposed a mechanistic model to explain the diverging effects of copper on the uncoupling activities of the different catechols.

Catechols↗
PubMedDate not supplied

[Hydrogenase activity in Thiocapsa roseopersicina according to the D2--H20 metabolic reaction].

Extracts of Thiocapsa roseopersicina cells show hydrogenase activity, measured by evolution of H2 from reduced methylviologene (MV) and by D2-H2O exchange reaction. According to these reactions the most part of hydrogenases is found to be in the soluble fraction. Hydrogenase activity measured in the exchange reaction is completely inhibited by p-chloromercurybenzoate (5-10- minus 3 M), iodacetate (1-10- minus 2 M) and 26% inhibited by KCN and o-phenanthroline (5-10- minus 3 M). Evolution of H2 from reduced MV was not inhibited by o-phenanthroline, KCN and iodacetate and was inhibited by 66% only with p-chloromercurybenzoate. Light and ATP stimulated hydrogenase activity of chromatophores did not affect on its activity in the soluble fraction. The results obtained show that there are certain differences in hydrogenase systems responsible for the exchange reaction and evolution of H2.

Adenosine Triphosphate↗
PubMedDate not supplied

[Participation of inorganic phosphates as electron donors in the primary reactions of photosynthesis in Rhodobacter sphaeroides].

The formation of ATP during photophosphorylation in chromatophores from purple nonsulfur bacterium Rhodobacter sphaeroides in the presence of phenazine methosulfate and without exogenous electron carriers under constant illumination and by the action of single light flashes was studied. It was shown that the photoinduced transport of electrons to the exogenous electron acceptor depends on phosphate. It was assumed that phosphate ions are electron donors in the reaction center P870; by the action of light, P870 converts the phosphate ion HPO4(2-) into anion radical HPO4-.. In the difference EPR spectra "light minus darkness" at 77 K, an asymmetrical doublet signal with a weak low-field line was observed. The signal had a g-tensor of about 2.014 and a hyperfine coupling constant of about 2.5 mT and belongs probably to the phosphate anion radical.

Adenosine Triphosphate↗