scholarly journals A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases

2011 ◽  
Vol 439 (3) ◽  
pp. 375-381 ◽  
Author(s):  
Leszek A. Kleczkowski ◽  
Matt Geisler ◽  
Elisabeth Fitzek ◽  
Malgorzata Wilczynska
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mobility ◽  
Regulatory Mechanism ◽  
Catalytic Domain ◽  
Evolutionary Relationships ◽  
Amino Acid Sequence Level ◽  
Significant Homology ◽  
Regulatory Functions

Plant pyrophosphorylases that are capable of producing UDP-sugars, key precursors for glycosylation reactions, include UDP-glucose pyrophosphorylases (A- and B-type), UDP-sugar pyrophosphorylase and UDP-N-acetylglucosamine pyrophosphorylase. Although not sharing significant homology at the amino acid sequence level, the proteins share a common structural blueprint. Their structures are characterized by the presence of the Rossmann fold in the central (catalytic) domain linked to enzyme-specific N-terminal and C-terminal domains, which may play regulatory functions. Molecular mobility between these domains plays an important role in substrate binding and catalysis. Evolutionary relationships and the role of (de)oligomerization as a regulatory mechanism are discussed.

scholarly journals Analysis of Htra Gene from Zebrafish (Danio Rerio)

2015 ◽  
Vol 10 (2) ◽  
Author(s):  
M. Murwantoko ◽  
Chio Oka ◽  
Masashi Kawaichi
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Danio Rerio ◽  
Serine Proteases ◽  
Catalytic Domain ◽  
Fruit Fly ◽  
Wide Range ◽  
Igf Binding ◽  
Bacterial Homolog

HtrA which is characterized by the combination of a trypsin-like catalytic domain with at least one C-terminalPDZ domain is a highly conserved family of serine proteases found in a wide range of organisms. However theidentified HtrA family numbers varies among spesies, for example the number of mammalian, Eschericia coli,fruit fly-HtrA family are 4, 3 and 1 gene respectively. One gene is predicted exist in zebrafish. Since no completeinformation available on zebrafish HtrA, in this paper zebrafish HtrA (zHtrA) gene was analyzed. The zHtrA isbelonged to HtrA1 member and predicted encodes 478 amino acids with a signal peptide, a IGF binding domain,a Kazal-type inhibitor domain in the up stream of HtrA-bacterial homolog. At the amino acid sequence the zHtrA1showed the 69%, 69%, 68%, 54% and 54% with the rat HtrA1, mouse HtrA1, human HtrA1, human HtrA3 andmouse HtrA4 respectively. The zHtrA1 is firstly expressed at 60 hpf and mainly in the vertebral rudiments in thetail region.

Nucleoid-associated proteins in Crenarchaea

2011 ◽  
Vol 39 (1) ◽  
pp. 116-121 ◽  
Author(s):  
Rosalie P.C. Driessen ◽  
Remus Th. Dame
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Structural Effect ◽  
Chromatin Organization ◽  
Large Set ◽  
Chromosomal Dna ◽  
Amino Acid Sequence Level ◽  
Generic Level ◽  
Architectural Proteins ◽  
Associated Proteins

Architectural proteins play an important role in compacting and organizing the chromosomal DNA in all three kingdoms of life (Eukarya, Bacteria and Archaea). These proteins are generally not conserved at the amino acid sequence level, but the mechanisms by which they modulate the genome do seem to be functionally conserved across kingdoms. On a generic level, architectural proteins can be classified based on their structural effect as DNA benders, DNA bridgers or DNA wrappers. Although chromatin organization in archaea has not been studied extensively, quite a number of architectural proteins have been identified. In the present paper, we summarize the knowledge currently available on these proteins in Crenarchaea. By the type of architectural proteins available, the crenarchaeal nucleoid shows similarities with that of Bacteria. It relies on the action of a large set of small, abundant and generally basic proteins to compact and organize their genome and to modulate its activity.

scholarly journals Purification, characterization, gene sequence, and significance of a bacterioferritin from Mycobacterium leprae.

1994 ◽  
Vol 180 (1) ◽  
pp. 319-327 ◽  
Author(s):  
M C Pessolani ◽  
D R Smith ◽  
B Rivoire ◽  
J McCormick ◽  
S A Hefta ◽  
...  
Keyword(s):  
Amino Acid ◽  
Membrane Protein ◽  
Amino Acid Sequence ◽  
Mycobacterium Leprae ◽  
Native Molecular Mass ◽  
Molecular Features ◽  
Ferroxidase Center ◽  
Considerable Homology

The study of tissue-derived Mycobacterium leprae provides insights to the immunopathology of leprosy and helps identify broad molecular features necessary for mycobacterial parasitism. A major membrane protein (MMP-II) of in vivo-derived M. leprae previously recognized (Hunter, S.W., B. Rivoire, V. Mehra, B.R. Bloom, and P.J. Brennan. 1990. J. Biol. Chem. 265:14065) was purified from extracts of the organism and partial amino acid sequence obtained. This information allowed recognition, within one of the cosmids that encompass the entire M. leprae genome, of a complete gene, bfr, encoding a protein of subunit size 18.2 kD. The amino acid sequence deduced from the major membrane protein II (MMP-II) gene revealed considerable homology to several bacterioferritins. Analysis of the native protein demonstrated the iron content, absorption spectrum, and large native molecular mass (380 kD) of several known bacterioferritins. The ferroxidase-center residues typical of ferritins were conserved in the M. leprae product. Oligonucleotides derived from the amino acid sequence of M. leprae bacterioferritin enabled amplification of much of the MMP-II gene and the detection of homologous sequences in Mycobacterium paratuberculosis, Mycobacterium avium, Mycobacterium tuberculosis, Mycobacterium intracellulare, and Mycobacterium scrofulaceum. The role of this iron-rich protein in the virulence of M. leprae is discussed.

scholarly journals Identification and characterization of DdPDE3, a cGMP-selective phosphodiesterase from Dictyostelium

2001 ◽  
Vol 353 (3) ◽  
pp. 635-644 ◽  
Author(s):  
Hidekazu KUWAYAMA ◽  
Helena SNIPPE ◽  
Mari DERKS ◽  
Jeroen ROELOFS ◽  
Peter J. M. VAN HAASTERT
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Catalytic Domain ◽  
Expressed Sequence Tag ◽  
Sequence Similarity ◽  
Second Messengers ◽  
Kinetic Properties ◽  
Intracellular Camp ◽  
Catalytic Domains ◽  
Dual Specificity

In Dictyostelium cAMP and cGMP have important functions as first and second messengers in chemotaxis and development. Two cyclic-nucleotide phosphodiesterases (DdPDE 1 and 2) have been identified previously, an extracellular dual-specificity enzyme and an intracellular cAMP-specific enzyme (encoded by the psdA and regA genes respectively). Biochemical data suggest the presence of at least one cGMP-specific phosphodiesterase (PDE) that is activated by cGMP. Using bioinformatics we identified a partial sequence in the Dictyostelium expressed sequence tag database that shows a high degree of amino acid sequence identity with mammalian PDE catalytic domains (DdPDE3). The deduced amino acid sequence of a full-length DdPDE3 cDNA isolated in this study predicts a 60kDa protein with a 300-residue C-terminal PDE catalytic domain, which is preceded by approx. 200 residues rich in asparagine and glutamine residues. Expression of the DdPDE3 catalytic domain in Escherichia coli shows that the enzyme has Michaelis–Menten kinetics and a higher affinity for cGMP (Km = 0.22µM) than for cAMP (Km = 145µM); cGMP does not stimulate enzyme activity. The enzyme requires bivalent cations for activity; Mn2+ is preferred to Mg2+, whereas Ca2+ yields no activity. DdPDE3 is inhibited by 3-isobutyl-1-methylxanthine with an IC50 of approx. 60µM. Overexpression of the DdPDE3 catalytic domain in Dictyostelium confirms these kinetic properties without indications of its activation by cGMP. The properties of DdPDE3 resemble those of mammalian PDE9, which also shows the highest sequence similarity within the catalytic domains. DdPDE3 is the first cGMP-selective PDE identified in lower eukaryotes.

Endorphines: structure, rôles et biogénèse

1981 ◽  
Vol 59 (5) ◽  
pp. 413-431
Author(s):  
M. Chrétien ◽  
N. G. Seidah ◽  
H. Scherrer
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Opiate Receptors ◽  
Endocrine Control ◽  
Pain Transmission ◽  
Starting Point ◽  
Polypeptide Hormones ◽  
Regulatory Functions ◽  
The Brain ◽  
Lipolytic Hormones

The knowledge of the amino acid sequence of both β-lipotropin (β-LPH) and γ-LPH was the starting point that led to the hypothesis, considered revolutionary in 1967, that hormonal precursors exist. This concept was simultaneously proposed for proinsulin and applied later to other polypeptide hormones. The discovery of endorphins brought together two fields of research that were not related: the opiates and the so-called pituitary lipotropic hormones. The demonstration of specific brain opiate receptors led to the hypothesis of the existence of endogenous opiate ligands which could act as neurotransmittors. The isolation of such substances in the brain, first named enkephalins, revealed through their amino acid sequence their structural homology with the pituitary lipolytic hormones. The finding of a more potent opioid substance in the pituitary (β-endorphin) that comprises the last 31 amino acids of β-LPH shed a new light on the hypothesis proposed earlier which gave to β-LPH a role as a precursor molecule. Finally, the addition of ACTH completed a putative multipotent precursor model that has been recently named pro-opiomelanocortin. Pulse–chase experiments have definitely proven that β-endorphin is a maturation product of a large precursor also containing ACTH and MSH. In other studies, many groups have suggested that endorphins play important roles as possible neuromodulators in pain transmission, in analgesia, in tolerance and dependance, as well as on behavior and endocrine regulations, mainly those related to the hypothalamo–pituitary axes. The elucidation of the biosynthetic process or processes of cerebral endorphins (either enkephalins or β-endorphin) is of primary importance in order to understand better their biological as well as regulatory functions. These studies should also be applicable to the biosynthesis of all the other neuronal peptide hormones. It is hoped that they will provide new tools for the study of some important central nervous system functions, such as pain and endocrine control and the physiopathology of behavioral diseases.

scholarly journals A Mono-2-Ethylhexyl Phthalate Hydrolase from a Gordonia sp. That Is Able To Dissimilate Di-2-Ethylhexyl Phthalate

2006 ◽  
Vol 72 (4) ◽  
pp. 2394-2399 ◽  
Author(s):  
Tuguhiro Nishioka ◽  
Makoto Iwata ◽  
Takuya Imaoka ◽  
Maiko Mutoh ◽  
Yoshihiro Egashira ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Contaminated Soil ◽  
Primary Structure ◽  
Independent Group ◽  
Serine Hydrolases ◽  
Cell Extracts ◽  
Significant Homology ◽  
Serine Esterases ◽  
Ethylhexyl Phthalate

ABSTRACT Gordonia sp. strain P8219, a strain able to decompose di-2-ethylhexyl phthalate, was isolated from machine oil-contaminated soil. Mono-2-ethylhexyl phthalate hydrolase was purified from cell extracts of this strain. This enzyme was a 32,164-Da homodimeric protein, and it effectively hydrolyzed monophthalate esters, such as monoethyl, monobutyl, monohexyl, and mono-2-ethylhexyl phthalate. The Km and V max values for mono-2-ethylhexyl phthalate were 26.9 ± 4.3 μM and 18.1 ± 0.9 μmol/min · mg protein, respectively. The deduced amino acid sequence of the enzyme exhibited less than 30% homology with those of meta-cleavage hydrolases which are serine hydrolases but exhibited no significant homology with the sequences of serine esterases. The pentapeptide motif GXSXG, which is conserved in serine hydrolases, was present in the sequence. The enzymatic properties and features of the primary structure suggested that this enzyme is a novel enzyme belonging to an independent group of serine hydrolases.

scholarly journals Complete structure of the hydrophilic domain in the porcine NADPH-cytochrome P-450 reductase

1986 ◽  
Vol 236 (3) ◽  
pp. 871-878 ◽  
Author(s):  
F Vogel ◽  
L Lumper
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Structural Data ◽  
Computer Assisted ◽  
Nadph Cytochrome ◽  
Positional Identity ◽  
Significant Homology ◽  
Assisted Analysis ◽  
Cytochrome P 450 ◽  
Hydrophilic Domain

The 622-residue amino acid sequence of the hydrophilic domain in the porcine NADPH-cytochrome P-450 reductase (EC 1.6.2.4) is reported. The structural data required to complete the sequences published previously [Vogel, Kaiser, Witt & Lumper (1985) Biol. Chem. Hoppe-Seyler 366, 577-587] and to establish the primary structure of the porcine hydrophilic domain have been obtained by sequencing proteolytic subfragments derived from CNBr fragments and by characterizing the overlapping S-[14C]methylmethionine-containing peptides isolated from tryptic digests of the [14C]methyl-labelled hydrophilic domain. The hydrophilic domain displays 91.8% positional identity with that of the corresponding domain in the rat NADPH-cytochrome P-450 reductase. The region Val528-Ser678 in the NADPH-cytochrome P-450 reductase shows a significant homology to the sequence Ile165-Tyr314 in the spinach ferredoxin-NADP+ oxidoreductase. A model for the secondary structure of the hydrophilic domain has been derived by computer-assisted analysis of the amino acid sequence. Cys472 and Cys566 are protected against chemical modification in the NADP+ complex of the NADPH-cytochrome P-450 reductase.

scholarly journals A role for the Fem-1 gene of Drosophila melanogaster in adult courtship

2020 ◽  
Author(s):  
Miles Thies ◽  
Brett Berke
Keyword(s):  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sex Determination ◽  
Mutational Analysis ◽  
Courtship Behavior ◽  
Evolutionary Relationships ◽  
Induced Mutations ◽  
C Elegans ◽  
Conserved Gene

The Fem family of genes influences sex determination and/or the development of sex-specific characteristics in a wide variety of organisms. Here, we describe the first mutational analysis of the Fem-1 gene of Drosophila melanogaster. The amino acid sequence of the two Drosophila Fem-1 transcripts are moderately conserved compared to that of both Fem-1 in C. elegans and the two Fem-1 transcripts in humans, with multiple ankyrin repeats. Using two transposon-induced mutations of Drosophila Fem-1, we observed striking defects in adult courtship behavior that are attributed to defects in male courting as opposed to female receptivity. Specifically, viable Fem-1 mutant males courted Fem-1 females more vigorously with an increased amount of chasing and singing than pairs of control flies. Nevertheless, Fem-1 males did not copulate at a higher frequency than controls. The above courtship defects persisted when Fem-1 males courted control females, but no phenotypes were observed when control males courted Fem-1 females. These results indicate that Drosophila Fem-1 may interact with other genes involved in courtship and sex determination. Fem-1 mutants also suppressed wing and body growth, consistent with the actions of a homologue in mice. Additional analyses of these Fem-1 alleles will help address the nature of these mutations, deepen our molecular understanding of courtship, and contribute to the evolutionary relationships among this highly conserved gene family.

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