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Article: Antifouling enzymes and the biochemistry of marine settlement.

Kristensen, Jakob Broberg / Meyer, Rikke Louise / Laursen, Brian Søgaard / Shipovskov, Stepan / Besenbacher, Flemming / Poulsen, Charlotte Horsmans

Biotechnology advances

2008 Volume 26, Issue 5, Page(s) 471–481

Abstract: Antifouling coatings are used extensively on marine vessels and constructions, but unfortunately they are found to pose a threat to the marine environment, notably due to content of metal-based biocides. Enzymes have repeatedly been proposed as an ... ...

Abstract	Antifouling coatings are used extensively on marine vessels and constructions, but unfortunately they are found to pose a threat to the marine environment, notably due to content of metal-based biocides. Enzymes have repeatedly been proposed as an alternative to traditional antifouling compounds. In this review, the enzymes claimed to hold antifouling activity are classified according to catalytic functions. The enzyme functions are juxtaposed with the current knowledge about the chemistry of settlement and adhesion of fouling organisms. Specific focus will be on bacteria, microalgae, invertebrate larvae and macroalgae zoospores. Two main concepts in enzyme-based antifouling are identified: breakdown of adhesive components and catalytic production of repellent compounds in-situ. The validity of the various modes of action is evaluated and the groups of enzymes with the highest potential are highlighted.
MeSH term(s)	Bacterial Adhesion/drug effects ; Biochemistry/trends ; Biofilms/drug effects ; Enzymes/chemistry ; Enzymes/pharmacology ; Equipment Contamination/prevention & control ; Marine Biology/methods ; Marine Biology/trends
Chemical Substances	Enzymes
Language	English
Publishing date	2008-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	47165-3
ISSN	0734-9750
ISSN	0734-9750
DOI	10.1016/j.biotechadv.2008.05.005
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Article: Biomimetic silica encapsulation of enzymes for replacement of biocides in antifouling coatings

Kristensen, Jakob Broberg / Besenbacher, Flemming / Kragh, Karsten Matthias / Laursen, Brian Søgaard / Meyer, Rikke Louise / Poulsen, Charlotte Horsmans

Green chemistry. 2010 Mar. 10, v. 12, no. 3

2010

Abstract: Current antifouling technologies for ship hulls are based on metals such as cuprous oxide and co-biocides like zinc pyrithione. Due to the persistent adverse environmental effects of these biocides, enzyme-based antifouling paints are proposed as a bio- ... ...

Abstract	Current antifouling technologies for ship hulls are based on metals such as cuprous oxide and co-biocides like zinc pyrithione. Due to the persistent adverse environmental effects of these biocides, enzyme-based antifouling paints are proposed as a bio-based, non-accumulating alternative. Here, a hydrogen peroxide-producing system composed of hexose oxidase (HOX, EC 1.1.3.5), glucoamylase (GA, EC 3.2.1.3) and starch is tested for the chemical and physical functionalities necessary for successful incorporation into a marine coating. The activity and stability of the enzymes in seawater was evaluated at different temperatures, and paint compatibility was assessed by measuring the distribution and activity of the enzymes incorporated into prototype coating formulations. We used a biomimetic encapsulation procedure for HOX through polyethylenimine-templated silica co-precipitation. The co-precipitation and formulation of a powder for mixing into a marine paint was performed in a one-step economical and gentle formulation process, in which silica co-precipitated HOX was combined with GA and starch to form the antifouling system. Silica co-precipitation significantly improved the stability and performance of the antifouling system in marine-like conditions. For example, encapsulation of HOX resulted in 46% higher activity at pH 8, and its stability in artificial seawater increased from retaining only 3.5% activity after 2 weeks to retaining 55% activity after 12 weeks. A coating comprising the full enzyme system released hydrogen peroxide at rates exceeding a target of 36 nmol cm−2 d−1 for 3 months in a laboratory assay, and had potential for prolonged action through incorporation in a self-polishing coating.
Keywords	antifouling agents ; biocides ; biomimetics ; coatings ; coprecipitation ; cuprous oxide ; encapsulation ; environmental impact ; glucan 1,4-alpha-glucosidase ; green chemistry ; hydrogen ; hydrogen peroxide ; metals ; mixing ; pH ; prototypes ; seawater ; silica ; starch ; temperature ; zinc pyrithione
Language	English
Dates of publication	2010-0310
Size	p. 387-394.
Publishing place	The Royal Society of Chemistry
Document type	Article
ZDB-ID	2006274-6
ISSN	1463-9270 ; 1463-9262
ISSN (online)	1463-9270
ISSN	1463-9262
DOI	10.1039/b913772f
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Article: Initiation of protein synthesis in bacteria.

Laursen, Brian Søgaard / Sørensen, Hans Peter / Mortensen, Kim Kusk / Sperling-Petersen, Hans Uffe

Microbiology and molecular biology reviews : MMBR

2005 Volume 69, Issue 1, Page(s) 101–123

Abstract: Valuable information on translation initiation is available from biochemical data and recently solved structures. We present a detailed description of current knowledge about the structure, function, and interactions of the individual components involved ...

Abstract	Valuable information on translation initiation is available from biochemical data and recently solved structures. We present a detailed description of current knowledge about the structure, function, and interactions of the individual components involved in bacterial translation initiation. The first section describes the ribosomal features relevant to the initiation process. Subsequent sections describe the structure, function, and interactions of the mRNA, the initiator tRNA, and the initiation factors IF1, IF2, and IF3. Finally, we provide an overview of mechanisms of regulation of the translation initiation event. Translation occurs on ribonucleoprotein complexes called ribosomes. The ribosome is composed of a large subunit and a small subunit that hold the activities of peptidyltransfer and decode the triplet code of the mRNA, respectively. Translation initiation is promoted by IF1, IF2, and IF3, which mediate base pairing of the initiator tRNA anticodon to the mRNA initiation codon located in the ribosomal P-site. The mechanism of translation initiation differs for canonical and leaderless mRNAs, since the latter is dependent on the relative level of the initiation factors. Regulation of translation occurs primarily in the initiation phase. Secondary structures at the mRNA ribosomal binding site (RBS) inhibit translation initiation. The accessibility of the RBS is regulated by temperature and binding of small metabolites, proteins, or antisense RNAs. The future challenge is to obtain atomic-resolution structures of complete initiation complexes in order to understand the mechanism of translation initiation in molecular detail.
MeSH term(s)	Bacteria/genetics ; Gene Expression Regulation, Bacterial ; Peptide Chain Initiation, Translational ; Protein Biosynthesis ; Ribosomes/genetics ; Ribosomes/metabolism
Language	English
Publishing date	2005-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1376131-6
ISSN	1098-5557 ; 1070-6275 ; 1092-2172
ISSN (online)	1098-5557 ; 1070-6275
ISSN	1092-2172
DOI	10.1128/MMBR.69.1.101-123.2005
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Article: The N-terminal domain (IF2N) of bacterial translation initiation factor IF2 is connected to the conserved C-terminal domains by a flexible linker.

Laursen, Brian Søgaard / Kjaergaard, Anne Cecillie / Mortensen, Kim Kusk / Hoffman, David W / Sperling-Petersen, Hans Uffe

Protein science : a publication of the Protein Society

2004 Volume 13, Issue 1, Page(s) 230–239

Abstract: Bacterial translation initiation factor IF2 is a multidomain protein that is an essential component of a system for ensuring that protein synthesis begins at the correct codon within a messenger RNA. Full-length IF2 from Escherichia coli and seven ... ...

Abstract	Bacterial translation initiation factor IF2 is a multidomain protein that is an essential component of a system for ensuring that protein synthesis begins at the correct codon within a messenger RNA. Full-length IF2 from Escherichia coli and seven fragments of the protein were expressed, purified, and characterized using nuclear magnetic resonance (NMR) and circular dichroism (CD) methods. Interestingly, resonances of the 6 kD IF2N domain located at the extreme N terminus of IF2 can be clearly identified within the NMR spectra of the full-length 97-kD protein. (15)N NMR relaxation rate data indicate that (1) the IF2N domain is internally well ordered and tumbles in solution in a manner that is independent of the other domains of the IF2 protein, and (2) the IF2N domain is connected to the C-terminal regions of IF2 by a flexible linker. Chemical shifts of resonances within the isolated IF2N domain do not significantly differ from those of the corresponding residues within the context of the full-length 97-kD protein, indicating that IF2N is a structurally independent unit that does not strongly interact with other regions of IF2. CD and NMR data together provide evidence that Domains I-III of IF2 have unstructured and flexible regions as well as substantial helical content; CD data indicate that the helical content of these regions decreases significantly at temperatures above 35 degrees C. The features of structurally well-ordered N- and C-terminal domains connected by a flexible linker with significant helical content are reminiscent of another translation initiation factor, IF3.
MeSH term(s)	Amino Acid Sequence ; Circular Dichroism ; Cloning, Molecular ; Computer Simulation ; Conserved Sequence ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/genetics ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/isolation & purification ; Escherichia coli Proteins/metabolism ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Nuclear Magnetic Resonance, Biomolecular ; Peptide Fragments/analysis ; Peptide Fragments/chemistry ; Prokaryotic Initiation Factor-2/chemistry ; Prokaryotic Initiation Factor-2/genetics ; Prokaryotic Initiation Factor-2/isolation & purification ; Prokaryotic Initiation Factor-2/metabolism ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Solutions/chemistry ; Temperature
Chemical Substances	Escherichia coli Proteins ; Peptide Fragments ; Prokaryotic Initiation Factor-2 ; Solutions
Language	English
Publishing date	2004-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1106283-6
ISSN	1469-896X ; 0961-8368
ISSN (online)	1469-896X
ISSN	0961-8368
DOI	10.1110/ps.03337604
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Article: A conserved structural motif at the N terminus of bacterial translation initiation factor IF2.

Laursen, Brian Søgaard / Mortensen, Kim Kusk / Sperling-Petersen, Hans Uffe / Hoffman, David W

The Journal of biological chemistry

2003 Volume 278, Issue 18, Page(s) 16320–16328

Abstract: The 18-kDa Domain I from the N-terminal region of translation initiation factor IF2 from Escherichia coli was expressed, purified, and structurally characterized using multidimensional NMR methods. Residues 2-50 were found to form a compact subdomain ... ...

Abstract	The 18-kDa Domain I from the N-terminal region of translation initiation factor IF2 from Escherichia coli was expressed, purified, and structurally characterized using multidimensional NMR methods. Residues 2-50 were found to form a compact subdomain containing three short beta-strands and three alpha-helices, folded to form a betaalphaalphabetabetaalpha motif with the three helices packed on the same side of a small twisted beta-sheet. The hydrophobic amino acids in the core of the subdomain are conserved in a wide range of species, indicating that a similarly structured motif is present at the N terminus of IF2 in many of the bacteria. External to the compact 50-amino acid subdomain, residues 51-97 are less conserved and do not appear to form a regular structure, whereas residues 98-157 form a helix containing a repetitive sequence of mostly hydrophilic amino acids. Nitrogen-15 relaxation rate measurements provide evidence that the first 50 residues form a well ordered subdomain, whereas other regions of Domain I are significantly more mobile. The compact subdomain at the N terminus of IF2 shows structural homology to the tRNA anticodon stem contact fold domains of the methionyl-tRNA and glutaminyl-tRNA synthetases, and a similar fold is also found in the B5 domain of the phenylalanine-tRNA synthetase. The results of the present work will provide guidance for the design of future experiments directed toward understanding the functional roles of this widely conserved structural domain within IF2.
MeSH term(s)	Amino Acid Motifs ; Amino Acid Sequence ; Circular Dichroism ; Conserved Sequence ; Epitope Mapping ; Escherichia coli Proteins/chemistry ; Molecular Sequence Data ; Nuclear Magnetic Resonance, Biomolecular ; Prokaryotic Initiation Factor-2/chemistry ; Protein Folding
Chemical Substances	Escherichia coli Proteins ; Prokaryotic Initiation Factor-2
Language	English
Publishing date	2003-02-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M212960200
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Article: RNA chaperone activity of translation initiation factor IF1.

Croitoru, Victor / Semrad, Katharina / Prenninger, Silvia / Rajkowitsch, Lukas / Vejen, Max / Laursen, Brian Søgaard / Sperling-Petersen, Hans Uffe / Isaksson, Leif A

Biochimie

2006 Volume 88, Issue 12, Page(s) 1875–1882

Abstract: Translation initiation factor IF1 is an indispensable protein for translation in prokaryotes. No clear function has been assigned to this factor so far. In this study we demonstrate an RNA chaperone activity of this protein both in vivo and in vitro. The ...

Abstract	Translation initiation factor IF1 is an indispensable protein for translation in prokaryotes. No clear function has been assigned to this factor so far. In this study we demonstrate an RNA chaperone activity of this protein both in vivo and in vitro. The chaperone assays are based on in vivo or in vitro splicing of the group I intron in the thymidylate synthase gene (td) from phage T4 and an in vitro RNA annealing assay. IF1 wild-type and mutant variants with single amino acid substitutions have been analyzed for RNA chaperone activity. Some of the IF1 mutant variants are more active as RNA chaperones than the wild-type. Furthermore, both wild-type IF1 and mutant variants bind with high affinity to RNA in a band-shift assay. It is suggested that the RNA chaperone activity of IF1 contributes to RNA rearrangements during the early phase of translation initiation.
MeSH term(s)	Amino Acid Substitution ; Electrophoretic Mobility Shift Assay ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Peptide Initiation Factors/genetics ; Peptide Initiation Factors/metabolism ; Protein Binding ; Protein Biosynthesis ; RNA/chemistry ; RNA/genetics ; RNA/metabolism ; RNA Splicing ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism
Chemical Substances	Molecular Chaperones ; Peptide Initiation Factors ; RNA-Binding Proteins ; RNA (63231-63-0)
Language	English
Publishing date	2006-12
Publishing country	France
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	120345-9
ISSN	0300-9084
ISSN	0300-9084
DOI	10.1016/j.biochi.2006.06.017
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Article: Structural requirements of the mRNA for intracistronic translation initiation of the enterobacterial infB gene.

Laursen, Brian Søgaard / de A Steffensen, Søren A / Hedegaard, Jakob / Moreno, Juan Manuel Palacios / Mortensen, Kim Kusk / Sperling-Petersen, Hans Uffe

Genes to cells : devoted to molecular & cellular mechanisms

2002 Volume 7, Issue 9, Page(s) 901–910

Abstract: Background: The gene infB encodes the prokaryotic translation initiation factor IF2, a central macromolecular component in the formation of the ribosomal 70S initiation complex. In Escherichia coli, infB encodes three forms of IF2: IF2alpha, IF2beta and ...

Abstract	Background: The gene infB encodes the prokaryotic translation initiation factor IF2, a central macromolecular component in the formation of the ribosomal 70S initiation complex. In Escherichia coli, infB encodes three forms of IF2: IF2alpha, IF2beta and IF2gamma. The expression of IF2beta and IF2gamma is a tandem translation from intact infB mRNA and not merely a translation of post-transcriptionally truncated mRNA. The molecular mechanism responsible for the ribosomal recognition of the two intracistronic translation initiation sites in E. coli infB is not well characterized. Results: We found three different forms of IF2 in Enterobacter cloacae, Klebsiella oxytoca, Salmonella enterica, Salmonella typhimurium, and two different forms in Proteus vulgaris. We identified the intracistronic translation initiation sites of the mRNA by isolation and N-terminal sequencing of the shorter isoforms of IF2 in S. enterica and S. typhimurium. A further search in the readily available public sequence databases revealed that infB from Yersinia pestis also contains an intracistronic in-frame initiation site used for the translation of IF2beta. The base composition in a part of the 5' end of the DNA coding strand of the enterobacterial infB gene shows a strong preference for adenine (A) over thymine (T) with a maximum ratio of A-to-T around the intracistronic initiation sites. We demonstrate that the mRNA has an open structure around the ribosomal binding region. Conclusion: Efficient intracistronic translation initiation of the infB gene is suggested to require an mRNA with this special base composition that results in an open, single-stranded structure at the ribosomal binding region.
MeSH term(s)	Bacterial Proteins/genetics ; Base Sequence ; Enterobacter/genetics ; Enterobacteriaceae/genetics ; Enterobacteriaceae/metabolism ; Genes, Bacterial ; Klebsiella oxytoca/genetics ; Molecular Sequence Data ; Nucleic Acid Conformation ; Peptide Chain Initiation, Translational ; Prokaryotic Initiation Factor-2/genetics ; Protein Biosynthesis ; Protein Isoforms/genetics ; Proteus vulgaris/genetics ; RNA, Bacterial/chemistry ; RNA, Bacterial/genetics ; RNA, Bacterial/metabolism ; RNA, Messenger/chemistry ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Salmonella enterica/genetics ; Sequence Alignment
Chemical Substances	Bacterial Proteins ; Prokaryotic Initiation Factor-2 ; Protein Isoforms ; RNA, Bacterial ; RNA, Messenger
Language	English
Publishing date	2002-09-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1330000-3
ISSN	1365-2443 ; 1356-9597
ISSN (online)	1365-2443
ISSN	1356-9597
DOI	10.1046/j.1365-2443.2002.00571.x
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Article: Characterization of mutations in the GTP-binding domain of IF2 resulting in cold-sensitive growth of Escherichia coli.

Laursen, Brian Søgaard / Siwanowicz, Igor / Larigauderie, Guilhem / Hedegaard, Jakob / Ito, Koreaki / Nakamura, Yoshikazu / Kenney, John M / Mortensen, Kim Kusk / Sperling-Petersen, Hans Uffe

Journal of molecular biology

2002 Volume 326, Issue 2, Page(s) 543–551

Abstract: The infB gene encodes translation initiation factor IF2. We have determined the entire sequence of infB from two cold-sensitive Escherichia coli strains IQ489 and IQ490. These two strains have been isolated as suppressor strains for the temperature- ... ...

Abstract	The infB gene encodes translation initiation factor IF2. We have determined the entire sequence of infB from two cold-sensitive Escherichia coli strains IQ489 and IQ490. These two strains have been isolated as suppressor strains for the temperature-sensitive secretion mutation secY24. The mutations causing the suppression phenotype are located within infB. The only variations from the wild-type (wt) infB found in the two mutant strains are a replacement of Asp409 with Glu in strain IQ489 and an insertion of Gly between Ala421 and Gly422 in strain IQ490. Both positions are located in the GTP-binding G-domain of IF2. A model of the G-domain of E.coli IF2 is presented in. Physiological quantities of the recombinant mutant proteins were expressed in vivo in E.coli strains from which the chromosomal infB gene has been inactivated. At 42 degrees C, the mutants sustained normal cell growth, whereas a significant decrease in growth rate was found at 25 degrees C for both mutants as compared to wt IF2 expressed in the control strain. Circular dichroism spectra were recorded of the wt and the two mutant proteins to investigate the structural properties of the proteins. The spectra are characteristic of alpha-helix dominated structure, and reveal a significant different behavior between the wt and mutant IF2s with respect to temperature-induced conformational changes. The temperature-induced conformational change of the wt IF2 is a two-state process. In a ribosome-dependent GTPase assay in vitro the two mutants showed practically no activity at temperatures below 10 degrees C and a reduced activity at all temperatures up to 45 degrees C, as compared to wt IF2. The results indicate that the amino acid residues, Asp409 and Gly422, are located in important regions of the IF2 G-domain and demonstrate the importance of GTP hydrolysis in translation initiation for optimal cell growth.
MeSH term(s)	Amino Acid Sequence ; Bacterial Proteins/metabolism ; Base Sequence ; Binding Sites ; Circular Dichroism ; Cloning, Molecular ; Cold Temperature ; Escherichia coli/genetics ; Escherichia coli/growth & development ; Escherichia coli/metabolism ; GTP Phosphohydrolases/metabolism ; Gene Expression Regulation, Bacterial ; Genetic Complementation Test ; Guanosine Triphosphate/metabolism ; In Vitro Techniques ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Plasmids ; Prokaryotic Initiation Factor-2/chemistry ; Prokaryotic Initiation Factor-2/genetics ; Prokaryotic Initiation Factor-2/metabolism ; Protein Conformation ; Protein Engineering ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/chemistry ; Restriction Mapping
Chemical Substances	Bacterial Proteins ; Prokaryotic Initiation Factor-2 ; Recombinant Proteins ; Guanosine Triphosphate (86-01-1) ; GTP Phosphohydrolases (EC 3.6.1.-)
Language	English
Publishing date	2002-11-20
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/s0022-2836(02)01367-0
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