Isolation and Characterization of a Defensin-Like Peptide (Coprisin) from the Dung Beetle, Copris tripartitus

The antibacterial activity of immune-related peptides, identified by a differential gene expression analysis, was investigated to suggest novel antibacterial peptides. A cDNA encoding a defensin-like peptide, Coprisin, was isolated from bacteria-immunized dung beetle, Copris tripartitus, by using differential dot blot hybridization. Northern blot analysis showed that Coprisin mRNA was up-regulated from 4 hours after bacteria injection and its expression level was reached a peak at 16 hours. The deduced amino acid sequence of Coprisin was composed of 80 amino acids with a predicted molecular weight of 8.6 kDa and a pI of 8.7. The amino acid sequence of mature Coprisin was found to be 79.1% and 67.4% identical to those of defensin-like peptides of Anomala cuprea and Allomyrina dichotoma, respectively. We also investigated active sequences of Coprisin by using amino acid modification. The result showed that the 9-mer peptide, LLCIALRKK-NH2, exhibited potent antibacterial activities against Escherichia coli and Staphylococcus aureus.

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Cloning and expression of the gene for periplasmic poly(vinyl alcohol) dehydrogenase from Sphingomonas sp. strain 113P3, a novel-type quinohaemoprotein alcohol dehydrogenase

Microbiology ◽

10.1099/mic.0.28848-0 ◽

2006 ◽

Vol 152 (7) ◽

pp. 1941-1949 ◽

Cited By ~ 22

Author(s):

Rie Hirota-Mamoto ◽

Ryoko Nagai ◽

Shinjiro Tachibana ◽

Masaaki Yasuda ◽

Akio Tani ◽

...

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Alcohol Dehydrogenase ◽

Vinyl Alcohol ◽

Ralstonia Eutropha ◽

Blot Hybridization ◽

Amino Acid Sequences ◽

Cloning And Expression ◽

Poly Vinyl Alcohol ◽

Dot Blot

A gene for periplasmic poly(vinyl alcohol) (PVA) dehydrogenase (PVADH) was cloned, based on the N-terminal amino acid sequence of the purified PVADH from Sphingomonas sp. 113P3 and the sequence of the gene for PVADH (pvaA, GenBank accession no. AB190288). The recombinant PVADH tagged with hexahistidine was expressed in Escherichia coli and purified to homogeneity. The recombinant enzyme had the same characteristics as the purified enzyme from Sphingomonas sp. strain 113P. In addition to PVA, the recombinant PVADH could oxidize glycols such as polypropylene glycols and 1,3-butane/cyclohexanediol and 2,4-pentanediol, but neither primary nor secondary alcohols. The amino acid sequence of the recombinant PVADH showed similarity with those of PVADH from Pseudomonas sp. strain VM15C, putative PVADHs from Azoarcus sp. EbN1, and Xanthomonas species (54–25 % identity), and the quinohaemoprotein alcohol dehydrogenases (QH-ADHs) from Comamonas testosteroni, Ralstonia eutropha and Pseudomonas putida (25–29 % identity). PVADHs from strains 113P3 and VM15C have a conserved superbarrel domain (SD), probable PQQ-binding amino acids in the SD and a haem-binding domain (HBD) (they should be designated QH-PVADHs), but the positions of the amino acid sequences for the HBD and SD are the reverse of those of QH-ADHs. A protein structure of QH-PVADHs is proposed. Results of dot-blot hybridization and RT-PCR indicated that the three genes encoding oxidized PVA hydrolase, PVADH and cytochrome c are expressed constitutively and form an operon.

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Detection of single peptide with only one amino acid modification via electronic fingerprinting using reengineered durable channel of Phi29 DNA packaging motor

Biomaterials ◽

10.1016/j.biomaterials.2021.121022 ◽

2021 ◽

pp. 121022

Author(s):

Long Zhang ◽

Miranda L. Gardner ◽

Lakmal Jayasinghe ◽

Michael Jordan ◽

Julian Aldana ◽

...

Keyword(s):

Amino Acid ◽

Dna Packaging ◽

Acid Modification ◽

Amino Acid Modification ◽

Dna Packaging Motor ◽

Single Peptide

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Two forms of poliovirus VPg result from amino acid modification of a single viral protein

Virology ◽

10.1016/0042-6822(84)90183-1 ◽

1984 ◽

Vol 136 (2) ◽

pp. 453-456 ◽

Cited By ~ 1

Author(s):

Oliver C. Richards ◽

Kathryn Morton ◽

Susan C. Martin ◽

Ellie Ehrenfeld

Keyword(s):

Amino Acid ◽

Viral Protein ◽

Acid Modification ◽

Amino Acid Modification

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Post-Translational Amino Acid Modification

Encyclopedia of Psychopharmacology ◽

10.1007/978-3-540-68706-1_4473 ◽

2010 ◽

pp. 1052-1052

Author(s):

R. Hamish McAllister-Williams ◽

Daniel Bertrand ◽

Hans Rollema ◽

Raymond S. Hurst ◽

Linda P. Spear ◽

...

Keyword(s):

Amino Acid ◽

Acid Modification ◽

Amino Acid Modification

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d‐amino acid modification protectsN‐Acetyl‐seryl‐aspartyl‐lysyl‐proline from physiological hydroxylation and increases its antifibrotic effects on hepatic fibrosis

IUBMB Life ◽

10.1002/iub.2037 ◽

2019 ◽

Vol 71 (9) ◽

pp. 1302-1312 ◽

Cited By ~ 2

Author(s):

Xutao Zhang ◽

Jiming Zhou ◽

Yichao Zhu ◽

Lei He ◽

Zhijun Pang ◽

...

Keyword(s):

Amino Acid ◽

Hepatic Fibrosis ◽

Acid Modification ◽

Amino Acid Modification

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Extending the working pH of nitrobenzene degradation using ultrasonic/heterogeneous Fenton to the alkaline range via amino acid modification

Chemosphere ◽

10.1016/j.chemosphere.2014.12.064 ◽

2015 ◽

Vol 139 ◽

pp. 632-637 ◽

Cited By ~ 16

Author(s):

Gamal M.S. ElShafei ◽

F.Z. Yehia ◽

O.I.H. Dimitry ◽

A.M. Badawi ◽

Gh. Eshaq

Keyword(s):

Amino Acid ◽

Heterogeneous Fenton ◽

Acid Modification ◽

Amino Acid Modification ◽

Alkaline Range

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The Primary Structure of Bacillus subtilis Acidic Ribosomal Protein B-L9Isolation and Characterization of Peptides and the Complete Amino Acid Sequence

The Journal of Biochemistry ◽

10.1093/oxfordjournals.jbchem.a132852 ◽

1980 ◽

Keyword(s):

Bacillus Subtilis ◽

Amino Acid ◽

Amino Acid Sequence ◽

Ribosomal Protein ◽

Primary Structure ◽

Complete Amino Acid Sequence ◽

Isolation And Characterization ◽

Protein B ◽

Acidic Ribosomal Protein

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Mutations in Bartonella bacilliformis gyrB Confer Resistance to Coumermycin A1

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.42.11.2906 ◽

1998 ◽

Vol 42 (11) ◽

pp. 2906-2913 ◽

Cited By ~ 14

Author(s):

James M. Battisti ◽

Laura S. Smitherman ◽

D. Scott Samuels ◽

Michael F. Minnick

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Cell Extract ◽

Natural Resistance ◽

Temperature Sensitive ◽

Bartonella Bacilliformis ◽

Reading Frame ◽

E Coli ◽

Isolation And Characterization ◽

Spontaneous Mutants

ABSTRACT This study describes the first isolation and characterization of spontaneous mutants conferring natural resistance to an antibiotic for any Bartonella species. The Bartonella bacilliformis gyrB gene, which encodes the B subunit of DNA gyrase, was cloned and sequenced. The gyrB open reading frame (ORF) is 2,079 bp and encodes a deduced amino acid sequence of 692 residues, corresponding to a predicted protein of ∼77.5 kDa. Sequence alignment indicates that B. bacilliformis GyrB is most similar to the GyrB protein from Bacillus subtilis (40.1% amino acid sequence identity) and that it contains the longest N-terminal tail (52 residues) of any GyrB characterized to date. The cloned B. bacilliformis gyrB was expressed in an Escherichia coli S30 cell extract and was able to functionally complement a temperature-sensitive E. coli Cour gyrB mutant (strain N4177). We isolated and characterized spontaneous mutants of B. bacilliformis resistant to coumermycin A1, an antibiotic that targets GyrB. Sequence analysis of gyrB from 12 Cour mutants ofB. bacilliformis identified single nucleotide transitions at three separate loci in the ORF. The predicted amino acid substitutions resulting from these transitions are Gly to Ser at position 124 (Gly124→Ser), Arg184→Gln, and Thr214→Ala or Thr214→Ile, which are analogous to mutated residues found in previously characterized resistant gyrB genes fromBorrelia burgdorferi, E. coli,Staphylococcus aureus, and Haloferax sp. The Cour mutants are three to five times more resistant to coumermycin A1 than the wild-type parental strain.

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