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G Hobom

Publications and source records attributed to G Hobom.

At least 55 records · Page 3Linked to original sources
PubMed1993

Molecular and biological characteristics of avian polyomaviruses: isolates from different species of birds indicate that avian polyomaviruses form a distinct subgenus within the polyomavirus genus.

The isolation and characterization of two avian polyomaviruses, from chicken (BFDV-2) and a parrot (BFDV-3), is reported. Both isolates are closely related to the non-mammalian polyomavirus budgerigar fledgling disease virus (BFDV) isolated from budgerigars (now called BFDV-1), and all three viral genomes are shown to have the same basic size of 4981 bp. A 151 bp insertion was, however, observed in the non-coding region of BFDV-2 which represented an exact duplication of the left half of the non-coding region, including the putative early promoter and amino terminus of the large T antigen. With a further 15 base pairs exchanged elsewhere throughout the three genomes, these viruses have distinct degrees of tropism for various avian species. The production of antibodies directed against a beta-galactosidase-large T antigen fusion protein of BFDV-1 is described. These antibodies detected the large T antigen, with an M(r) of approximately 80K, and the small t antigen, with an M(r) of approximately 24K, in cells infected with BFDV isolates. Whereas these antibodies bind with low affinity to the large T antigen of simian virus 40 (SV40), SV40- or mouse polyomavirus-specific antibodies will not bind to the BFDV large T antigen. Antibodies directed against BFDV structural polypeptides exhibit broad, reciprocal cross-reactivities with all three structural proteins of mammalian polyomaviruses. The significance of polyomavirus infections in various avian species is discussed. Based on unique structural and biological properties we propose that these viruses should be placed in a distinct subgenus (Avipolyomavirus) within the polyomaviruses.

Animals↗
PubMed1992

Trans-splicing of an early embryo mRNA in Litomosoides carinii, coding for the major microfilarial sheath protein gp22.

Both genomic and cDNA clones have been isolated encoding the major sheath glycoprotein, gp22, of Litomosoides carinii microfilariae. The mature gp22 mRNA is shown to result from both trans-splicing of a 22-nucleotide 5'-leader sequence to an acceptor site at position 313 of the pre-mRNA, immediately upstream from the start codon, and from cis-splicing of a 117-nt intron located within the coding sequence. Cis-splicing precedes the trans-splicing reaction. The gp22 reading frame of 148 codons has the inferred structure of a prepro-protein and includes a leader peptide and a pro-segment ahead of the known N terminus of the mature, extracellular protein of 105 amino acids. The N-terminal part of that protein contains five repeats of an elastin-related pentapeptide sequence, which, together with a proline-threonine segment between two Cys clusters in the center and at its C terminus, may cause an elongated conformation with an apparent molecular size of 22 kDa in contrast to the calculated M(r) of 11,200.

Amino Acid Sequence↗
PubMed1991

Genomic organization of the bovine alpha-S1 casein gene.

We report the sequence of the complete bovine alpha-s1 casein gene eludicating for the first time the genomic organization of an alpha-s type casein gene. Extending over 17508 bp the gene is split into 19 exons, ranging in size from 24 bp to 385 bp. Except for the translational stop codon not a single coding triplet of the alpha-s1 reading frame is disrupted by any of the splice junctions, which all confirm to known splice consensus sequences. Nine out of 16 coding exons begin with a 'GAX' codon, specific for glutamate. Splicing of this codon from exon 10 to the preceding exon creates a major phosphorylation site. An intron-exon-intron stretch of 154 bp comprising exons 10 and 13 is found precisely duplicated. Associated with the gene, copies of 8 atriodactyla retroposons are found, 6 of which are interspersed into the sequences of the three longest introns. We discuss the possibility that three functional parts of the gene have been recruited and evolutionary conserved at a time before gene diversification gave rise to the separate evolution of alpha- and beta-type casein-genes.

Animals↗
PubMed1991

Nuclear localization of budgerigar fledgling disease virus capsid protein VP2 is conferred by residues 308-317.

The capsid protein VP2 of budgerigar fledgling disease virus (BFDV) contains two sequences (residues 309-315 and 334-340) which are homologous to the prototypic nuclear localization sequence (NLS) of the simian virus 40 T-antigen. Using recombinant potential NLS-beta-galactosidase fusion proteins we identified amino acid residues 308-317 (VPKRKRKLPT) to be the NLS of BFDV capsid proteins VP2 and VP3. Microfluorometry studies show that the BFDV-VP2 signal is considerably more efficient in nuclear transport kinetics, than the NLS of SV40-VP2, corresponding to amino acid residues 317-326 (PNKKKRKLSR).

Amino Acid Sequence↗
PubMed1988

Expression of viral hemagglutinin on the surface of E. coli.

Expression of a foreign protein molecule on the E. coli bacterial surface has been achieved through hybrid plasmid construction of fusion proteins using outer membrane protein ompA as a carrier system. Influenza virus hemagglutinin fusion proteins of this character have been shown to become integrated into the bacterial outer membrane and to expose their hemagglutinin moiety at the exterior surface in a conformation which is at least similar to the authentic viral antigen structure.

Bacterial Outer Membrane Proteins↗
PubMed1988

The genome of budgerigar fledgling disease virus, an avian polyomavirus.

Budgerigar fledgling disease virus (BFDV) represents the first avian member of the Polyomavirus family. In contrast to mammalian polyomaviruses BFDV exhibits unique biological properties, in particular it is able to cause an acute disease with distinct organ manifestations in affected birds. Here we present the complete nucleotide sequence of the BFDV genome, consisting of 4980 bp. When compared to published nucleotide sequences of other polyomaviruses, the BFDV genome exposes a number of very similar structural features, and undoubtedly qualifies as a member of that family of viruses. The most important differences include a large T antigen remarkably reduced in size, and an origin of replication region with fundamental deviations from the origin structure of all other polyomaviruses. The specific characteristics of the BFDV genome may be used to place this virus into a distinct subgroup within the Polyomavirus family and may give a clue to the elucidation of its extraordinary biological properties.

Amino Acid Sequence↗
PubMed1984

Eight new restriction endonucleases fröm Herpetosiphon giganteus--divergent evolution in a family of enzymes.

Characterization of eight restriction endonucleases isolated from five strains of Herpetosiphon giganteus is described. HgiCI from strain Hpg9 recognizes and cleaves the degenerate sequence: GGPyPuCC, producing 5'-hexanucleotide protruding ends. Endonucleases HgiBI, HgiCII and HgiEI are isoschizomers of AvaII; HgiCIII and HgiDII are isoschizomers of SalI; and HgiDI and HgiGI are isoschizomers of AcyI. Based upon their closely related and in part overlapping recognition specificities a close evolutionary relationship is proposed for all known Hgi restriction endonucleases.

Base Sequence↗
PubMed1984

The nucleotide recognized by the Escherichia coli A restriction and modification enzyme.

The nucleotide recognition sequence for the restriction-modification enzyme of Escherichia coli A (EcoA) has been determined to be GAG-7N-GTCA. This sequence is fairly similar, but distinctly different from the two other type I restriction enzyme recognition sites known for E. coli B and E. coli K12, respectively. N6-adenosine methylation has been observed at nucleotide positions 2 and 12 within that sequence after modification by EcoA. As a reference point for mapping the single EcoA site in lambda, the position of lambda point mutation Oam29 has been determined also.

Base Sequence↗
PubMed1982

The rex region of bacteriophage lambda: two genes under three-way control.

The nucleotide sequence of the phage lambda rex region consists of 1428 bp and codes for two genes, rexA and rexB. Hence the complete lambda immunity region codes for four genes and covers 2664 bp of sequence unique to lambda, as defined by the left and right boundaries of the imm434 region. Coordinate expression of both rexA and rexB, which are co-regulated with the cI repressor gene from promoters p rm and p re is responsible for the Rex phenotype, i.e. exclusion of a wide variety of superinfecting phage such as T4rII. The position of a third promoter, p lit, which overlaps the carboxy-terminal end of the rexA coding region, permits expression of rexB without rexA, from the resulting 470 nucleotide lit RNA. The lit transcript, therefore, must act as messenger for rexB in the noncoordinate expression of the rex genes that occurs late in lambda lytic infection. The coordinate and noncoordinate expression of rexB and rexA suggests a dual role for the very hydrophobic rexB protein. Studies of lambda early and late DNA replication implicate rexB as having auxiliary functions in both lysogenisation and lytic infection.

Bacteriophage lambda↗
PubMed1982

A chain of interlinked genes in the ninR region of bacteriophage lambda.

The 3612-bp DNA sequence of the phage lambda P-Q (ninR) region contains a series of nine open reading frames in a distinctly overlapping pattern: ATGA sequence modules occur at the boundaries of consecutive genes and are able to serve both as terminator (TGA) and (re)initiator (ATG) codons for most of the adjacent frames. Together with genes O, P, and Q, the newly detected ren and ninA through ninH constitute a series of twelve closely linked genes in the pR operon. Based upon the available evidence for several of the nin proteins, and on plasmid expression data, we conclude that at least the larger nin genes, and probably all of the newly detected open reading frames code for proteins. The nin5 deletion of 2803 bp is a frame-to-frame fusion of ren and ninH, and covers the t R2 termination signal located near its left boundary, immediately behind the ren gene. The possible significance of the observed chain of closely interlinked genes for the regulation of Q expression is discussed.

Bacteriophage lambda↗
PubMed1981

Restriction endonuclease EcaI from Enterobacter cloacae.

Restriction endonuclease EcaI obtained from Enterobacter cloacae DSM30056 recognizes the group of heptanucleotide palindromes 5'-G[unk]G-T-N-A-C-C-3', and on cleavage (arrow) produces fragments with 5'-terminal pentanucleotide extensions. It is identical in specificity with restriction endonuclease BstEII from Bacillus stearothermophilus ET.

Base Sequence↗
PubMed1981

ClaI. a new restriction endonuclease from Caryophanon latum L.

From Caryophanon latum L site specific restriction endonuclease (ClaI) has been purified, which recognises tha DNA hexanucleotide palindrome 5'-A-T-C-G-A-T-3'. Staggered cleavage generates DNA restriction fragments with 5'-terminal pCG extensions. A CLaI map of bacteriophage lambda has been determined, which indicates cleavage inhibition due to adenine methylation at over lapping ClaI-GATC recognition sequences. Plasmid pBR322 is cut only once, in the tetracycline promoter region, and can, therefore, be used as a vector system for cloning fragments derived from ClaI digestions, and in addition for fragments generated by TaqI, HpaII, and several other enzymes.

Bacteriophage lambda↗
PubMed1981

[Topicalities from gene technology. Protein synthesized by bacteria the better therapeutic alternative (author's transl)].

Compared with conventional methods for obtaining highly complicated natural substances such as peptide hormones and vaccine antibodies from animal or human tissues or cell culture, the synthesis of these therapeutically important substances in bacterial cells, made possible by gene technology, has the decisive advantage that the bacteria synthesize exclusively that protein whose appropriate genetic information has previously been obtained and insinuated into the bacterial cell under accurately controlled physicochemical conditions. Thus, the mmammalian protein produced in bacteria is purer and consequently freer from side-effects than material obtained from ammmalian cells.

Animals↗