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Article: Phage misplay.

Rasched, I

Bio/technology (Nature Publishing Company)

1995 Volume 13, Issue 2, Page(s) 105

MeSH term(s)	Biotechnology/methods ; Coliphages/genetics ; Coliphages/physiology ; Inovirus/genetics ; Inovirus/physiology
Language	English
Publishing date	1995-02
Publishing country	United States
Document type	Comment ; Letter
ZDB-ID	46225-1
ISSN	0733-222X
ISSN	0733-222X
DOI	10.1038/nbt0295-105b
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Zs.A 2167: Show issues

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Article: Purification and Characterization of Extracellular Pectinesterases from Phytophthora infestans.

Förster, H / Rasched, I

Plant physiology

2006 Volume 77, Issue 1, Page(s) 109–112

Abstract: Constitutively produced extracellular pectinesterases from culture filtrates of the potato late blight fungus Phytophthora infestans were purified and characterized. One enzyme (PE II) was purified to homogeneity. Sodium dodecyl sulfate electrophoresis ... ...

Abstract	Constitutively produced extracellular pectinesterases from culture filtrates of the potato late blight fungus Phytophthora infestans were purified and characterized. One enzyme (PE II) was purified to homogeneity. Sodium dodecyl sulfate electrophoresis of the second enzyme (PE I) revealed two protein bands; there are indications that both proteins are pectinesterases, which were not separable by a number of different techniques. Thus, P. infestans might produce three pectinesterases in vitro. Enzyme activities were optimal in the neutral pH range and were largely dependent on the presence of NaCl or CaCl(2) in the reaction medium. The molecular weight of the PE I-complex was between 45 and 48 kilodaltons, and the one of PE II was between 35 and 40 kilodaltons. Further investigations will help us to clarify the role of these enzymes during pathogenesis.
Language	English
Publishing date	2006-04-28
Publishing country	United States
Document type	Journal Article
ZDB-ID	208914-2
ISSN	1532-2548 ; 0032-0889
ISSN (online)	1532-2548
ISSN	0032-0889
DOI	10.1104/pp.77.1.109
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Article: The adsorption protein of filamentous phage fd: assignment of its disulfide bridges and identification of the domain incorporated in the coat.

Kremser, A / Rasched, I

Biochemistry

1994 Volume 33, Issue 46, Page(s) 13954–13958

Abstract: The mature adsorption protein (g3p) of filamentous phage fd consists of 406 amino acids. It contains eight cysteine residues in total. To determine the disulfide bond pattern, purified g3p was proteolytically digested, and the resulting peptides were ... ...

Abstract	The mature adsorption protein (g3p) of filamentous phage fd consists of 406 amino acids. It contains eight cysteine residues in total. To determine the disulfide bond pattern, purified g3p was proteolytically digested, and the resulting peptides were separated using RP-HPLC. N-terminal sequencing and mass spectrometry of cysteine-containing fragments showed that each cysteine is involved in an intramolecular disulfide bond. The cystine sites are Cys7-Cys36, Cys46-Cys53, Cys188-Cys201, and Cys354-Cys371. In the native conformation of g3p, none of the disulfide bridges is accessible to alkylating agents after treatment with DTT. The cystine sites seem therefore to be located in the interior of the folded molecule or are shielded by components of the phage envelope. The part of g3p which is incorporated in the phage coat and hence is inaccessible to proteolytic cleavage was identified after treatment of phage particles with subtilisin: Immunoblots performed with antibody directed against g3p revealed essentially one g3p fragment with an apparent molecular weight of approximately 17,000 which resisted the proteolytic attack. The amino terminus of this peptide was determined to be glycine 254. This amino acid position correlates with the carboxy-terminal end of the second glycine-rich region (amino acids 218-256) in the primary structure of g3p. The notion that the extended carboxy-terminal g3p fragment is indeed entirely buried within the phage envelope is further supported by the fact that only polyclonal antibodies raised against purified g3p are able to react with this peptide, whereas those against phage coat-associated g3p are not.
MeSH term(s)	Alkylating Agents ; Amino Acid Sequence ; Capsid/chemistry ; Capsid Proteins ; Cysteine/analysis ; DNA-Binding Proteins/chemistry ; Disulfides/analysis ; Inovirus ; Molecular Sequence Data ; Oxidation-Reduction ; Thermolysin ; Viral Fusion Proteins ; Viral Proteins/chemistry
Chemical Substances	Alkylating Agents ; Capsid Proteins ; DNA-Binding Proteins ; Disulfides ; Viral Fusion Proteins ; Viral Proteins ; Thermolysin (EC 3.4.24.27) ; Cysteine (K848JZ4886)
Language	English
Publishing date	1994-11-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi00250a051
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Zs.A 217: Show issues

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Article: The adsorption protein of bacteriophage fd and its neighbour minor coat protein build a structural entity.

Gailus, V / Rasched, I

European journal of biochemistry

1994 Volume 222, Issue 3, Page(s) 927–931

Abstract: The adsorption protein g3p and another minor coat protein, g6p, are located at one end of the filamentous bacteriophage fd [Grant, R.A., Lin, T.C., Konigsberg, W.E. & Webster, R.E. (1981) J. Biol. Chem. 256, 539-546]. Both proteins, representing the ... ...

Abstract	The adsorption protein g3p and another minor coat protein, g6p, are located at one end of the filamentous bacteriophage fd [Grant, R.A., Lin, T.C., Konigsberg, W.E. & Webster, R.E. (1981) J. Biol. Chem. 256, 539-546]. Both proteins, representing the proximal tip, were detached as an entity by a technique that allowed for gentle solubilization. Disrupting the phage particle with the detergent sodium deoxycholate and chloroform dissociates the major coat protein g8p, frees the phage DNA, but leaves g3p and g6p associated with each other. The g3p-g6p complex, which we termed the adsorption complex, and an oligomeric form of g3p with lower molecular mass were isolated and purified by gel-filtration chromatography in the presence of deoxycholate. These different oligomeric structures of g3p showed a different mobility in non-denaturing polyacrylamide-gel electrophoresis. Both forms were also found in non-denaturing polyacrylamide-gel electrophoresis from deoxycholate- and Triton-X-100-solubilized phage without prior chromatographic separation. The two oligomeric forms of g3p are composed of two g3p polypeptide chains in the case of the low-molecular-mass species, and four g3p and four g6p polypeptide chains for the adsorption complex.
MeSH term(s)	Capsid/chemistry ; Capsid/isolation & purification ; Capsid/metabolism ; Capsid Proteins ; Chromatography, Gel ; Cross-Linking Reagents ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/isolation & purification ; DNA-Binding Proteins/metabolism ; Electrophoresis, Polyacrylamide Gel ; Immunoblotting ; Inovirus/chemistry ; Molecular Weight ; Octoxynol/chemistry ; Viral Fusion Proteins ; Viral Proteins/chemistry ; Viral Proteins/isolation & purification ; Viral Proteins/metabolism
Chemical Substances	Capsid Proteins ; Cross-Linking Reagents ; DNA-Binding Proteins ; Viral Fusion Proteins ; Viral Proteins ; Octoxynol (9002-93-1)
Language	English
Publishing date	1994-06-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3032-6
ISSN	1432-1033 ; 0014-2956
ISSN (online)	1432-1033
ISSN	0014-2956
DOI	10.1111/j.1432-1033.1994.tb18941.x
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Zs.A 260: Show issues

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Article: Genetic analysis of the transfer region of the IncN plasmid N3.

Glocker, B / Rasched, I

Research in microbiology

1990 Volume 141, Issue 6, Page(s) 621–631

Abstract: Using lambda::Tn5 insertion mutagenesis and screening for conjugation, the boundaries of the IncN plasmid N3 transfer region were determined. Sensitivity to phage IKe infection was used to monitor that part of the N3 transfer region which harbours genes ... ...

Abstract	Using lambda::Tn5 insertion mutagenesis and screening for conjugation, the boundaries of the IncN plasmid N3 transfer region were determined. Sensitivity to phage IKe infection was used to monitor that part of the N3 transfer region which harbours genes for pilus synthesis and assembly. We cloned this region, creating plasmid pBG21. Escherichia coli cells transformed with pBG21 became sensitive to phage IKe and produced pili, as shown by electron microscopy. Various plasmid constructions containing parts of the pilus-encoding region were used for expression in a minicell system and for expression in an in vitro translation system, thus characterizing for the first time some of the gene products of domain I (Winans and Walker, 1985a) of the transfer region.
MeSH term(s)	Conjugation, Genetic ; DNA Transposable Elements ; Escherichia coli/cytology ; Escherichia coli/genetics ; Fimbriae, Bacterial ; In Vitro Techniques ; Plasmids/genetics ; Transfection/genetics
Chemical Substances	DNA Transposable Elements
Language	English
Publishing date	1990-07
Publishing country	France
Document type	Journal Article
ZDB-ID	1004220-9
ISSN	1769-7123 ; 0923-2508
ISSN (online)	1769-7123
ISSN	0923-2508
DOI	10.1016/0923-2508(90)90057-w
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Zs.A 890: Show issues

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Article: Convergent evolution of amino acid usage in archaebacterial and eubacterial lineages adapted to high salt.

Gandbhir, M / Rasched, I / Marlière, P / Mutzel, R

Research in microbiology

1995 Volume 146, Issue 2, Page(s) 113–120

Abstract: Chemical composition and physical properties of the total protein of Haloferax mediterranei, a halophilic archaebacterium requiring high salt concentration for growth, of Halomonas elongata, a halotolerant eubacterium able to grow at any concentration of ...

Abstract	Chemical composition and physical properties of the total protein of Haloferax mediterranei, a halophilic archaebacterium requiring high salt concentration for growth, of Halomonas elongata, a halotolerant eubacterium able to grow at any concentration of salt, and of Escherichia coli B, a eubacterium related to H. elongata, unable to grow at high salt concentration, were compared using robust standard biochemical methods. The distribution of amino acid abundancies in the bulk protein from H. elongata was found to be intermediate between that from H. mediterranei and that from E. coli. The two high-salt-adapted organisms displayed an enrichment in aspartic acid and glutamic acid together with an impoverishment in lysine as compared to E. coli. This signature in amino acid usage is reflected in the charge distribution of proteins, as revealed by anion exchange chromatography of crude cell extracts. Since H. elongata diverged from H. mediterranei more than three billion years ago, the resemblance of their amino acid usages can be interpreted as a convergent imprint of their common habitats onto the chemical constitution of their proteins.
MeSH term(s)	Archaea/chemistry ; Archaea/growth & development ; Archaea/metabolism ; Arginine/metabolism ; Aspartic Acid/metabolism ; Bacterial Proteins/chemistry ; Chromatography, DEAE-Cellulose ; Chromatography, Ion Exchange ; Escherichia coli/chemistry ; Escherichia coli/growth & development ; Escherichia coli/metabolism ; Eubacterium/chemistry ; Eubacterium/growth & development ; Eubacterium/metabolism ; Glutamic Acid/metabolism ; In Vitro Techniques ; Lysine/metabolism ; Oceans and Seas ; Sodium Chloride/metabolism
Chemical Substances	Bacterial Proteins ; Aspartic Acid (30KYC7MIAI) ; Glutamic Acid (3KX376GY7L) ; Sodium Chloride (451W47IQ8X) ; Arginine (94ZLA3W45F) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	1995-02
Publishing country	France
Document type	Journal Article
ZDB-ID	1004220-9
ISSN	1769-7123 ; 0923-2508
ISSN (online)	1769-7123
ISSN	0923-2508
DOI	10.1016/0923-2508(96)80889-8
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Article: Purification and characterization of a novel acid-soluble nuclear protein from developing embryos of the camel tick Hyalomma dromedarii (Acarina: Ixodidae).

Ibrahim, M A / Hamed, R R / Rasched, I

Biochimica et biophysica acta

1995 Volume 1249, Issue 1, Page(s) 79–85

Abstract: A novel acid-soluble protein has been extracted from nuclei of developing embryos of H. dromedarii ticks and purified to homogeneity. This tick embryo basic protein (TEBP) was predominant during the cleavage stage of tick embryogenesis, whereas the ... ...

Abstract	A novel acid-soluble protein has been extracted from nuclei of developing embryos of H. dromedarii ticks and purified to homogeneity. This tick embryo basic protein (TEBP) was predominant during the cleavage stage of tick embryogenesis, whereas the complete set of histones was detectable at the late cleavage stage. The amount of TEBP reaches a maximum value at day 9 after oviposition. Thereafter, the original N-terminal dipeptide (leucine-serine) is eliminated. This coincides with the start of organogenesis. In spite of its low molecular mass, TEBP seems to be related to histone H1 in some properties such as solubility in perchloric acid and binding affinity to DNA. A task for the future will be to define the role of this protein as a counterpart of the histones for the genome organization during embryogenesis.
MeSH term(s)	Amino Acid Sequence ; Animals ; Arthropod Proteins ; Camelus/parasitology ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/isolation & purification ; Molecular Sequence Data ; Nuclear Proteins/chemistry ; Nuclear Proteins/isolation & purification ; Ticks/embryology
Chemical Substances	Arthropod Proteins ; DNA-Binding Proteins ; Nuclear Proteins ; TEBP protein, Hyalomma dromedarii
Language	English
Publishing date	1995-05-18
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/0167-4838(95)00068-6
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Article: Ff coliphages: structural and functional relationships.

Rasched, I / Oberer, E

Microbiological reviews

1986 Volume 50, Issue 4, Page(s) 401–427

MeSH term(s)	Coliphages/genetics ; Coliphages/physiology ; Coliphages/ultrastructure ; DNA Replication ; DNA, Viral/analysis ; Genes, Viral ; Protein Biosynthesis ; Transcription, Genetic ; Viral Proteins/genetics ; Virus Replication
Chemical Substances	DNA, Viral ; Viral Proteins
Language	English
Publishing date	1986-12
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	6864-0
ISSN	0146-0749
ISSN	0146-0749
DOI	10.1128/mr.50.4.401-427.1986
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Ud II Zs.96: Show issues

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Article: Interchangeability of the adsorption proteins of bacteriophages Ff and IKe.

Endemann, H / Gailus, V / Rasched, I

Journal of virology

1993 Volume 67, Issue 6, Page(s) 3332–3337

Abstract: The wild-type adsorption protein (g3p) of filamentous phage IKe cannot be exchanged with its analogous protein in the related Ff (M13, fd, and f1) phage particles. Deletion mutants of the protein, however, are assembled into Ff phage particles. These ... ...

Abstract	The wild-type adsorption protein (g3p) of filamentous phage IKe cannot be exchanged with its analogous protein in the related Ff (M13, fd, and f1) phage particles. Deletion mutants of the protein, however, are assembled into Ff phage particles. These hybrid Ff phage particles bearing deleted IKe g3p attach to N pili, thus conserving the host attachment property of the protein but not its infection-initiating function. This means that the attachment specificity is determined by IKe g3p independently of other phage components in contact with it. Infection initiation function, the process in which phage DNA is released into the host, in contrast seems to require either more complex structural features of the protein (for example, a certain oligomeric structure) provided only in the original particle, or a concerted action of g3p with another particle component, not replaceable by its homologous counterpart in the related phage.
MeSH term(s)	Amino Acid Sequence ; Binding, Competitive ; Coliphages/genetics ; Coliphages/growth & development ; Escherichia coli ; Genetic Complementation Test ; Kanamycin Resistance ; Molecular Sequence Data ; Receptors, Virus ; Sequence Homology, Amino Acid ; Tetracycline Resistance ; Transduction, Genetic ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Virulence
Chemical Substances	Receptors, Virus ; Viral Proteins ; gene 3 protein, Enterobacteria phage Ike
Language	English
Publishing date	1993-06
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.67.6.3332-3337.1993
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Zs.A 609: Show issues

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Article: The lysine residues implicated in the gene 5 protein association sites.

Bayne, S / Rasched, I

Bioscience reports

1983 Volume 3, Issue 5, Page(s) 469–474

Abstract: Gene 5 protein, a DNA unwinding protein encoded by the bacteriophage fd, is self-associative in presence of DNA or oligonucleotides. The lysine residues implicated in the protein-protein binding domains have been identified after modification with ... ...

Abstract	Gene 5 protein, a DNA unwinding protein encoded by the bacteriophage fd, is self-associative in presence of DNA or oligonucleotides. The lysine residues implicated in the protein-protein binding domains have been identified after modification with acetimidate by means of peptide and amino acid analyses. These residues are Lys-7 and Lys-69.
MeSH term(s)	Amino Acid Sequence ; Coliphages/genetics ; DNA Helicases/metabolism ; DNA Replication ; DNA, Viral/metabolism ; Escherichia coli/genetics ; Imidoesters/pharmacology ; Indicators and Reagents/pharmacology ; Lysine ; Protein Binding ; Viral Proteins/metabolism
Chemical Substances	DNA, Viral ; Imidoesters ; Indicators and Reagents ; Viral Proteins ; ethyl acetimidate (1000-84-6) ; DNA Helicases (EC 3.6.4.-) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	1983-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	764946-0
ISSN	1573-4935 ; 0144-8463
ISSN (online)	1573-4935
ISSN	0144-8463
DOI	10.1007/bf01121958
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