Repair of Deoxyribonucleic Acid in
            <i>Haemophilus influenzae</i>
            I. X-Ray Sensitivity of Ultraviolet-sensitive Mutants and Their Behavior as Hosts to Ultraviolet-irradiated Bacteriophage and Transforming Deoxyribonucleic Acid

Setlow, Jane K.; Brown, Dianne C.; Boling, M.E.; Mattingly, Alice; Gordon, Milton P.

doi:10.1128/jb.95.2.546-558.1968

Cited by 180 publications

(87 citation statements)

References 16 publications

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“…By contrast, the transduction frequencies of the terials and Methods cml-r and tet-r markers in MS3878 were approximately the same between the UV-sensitive mutants and the original strains (Table 2). From these results, it was concluded that the UV-sensitive mutants were the recombinationdeficient type mutants as reported for the recmutants (5,11,22,25).…”

supporting

confidence: 62%

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Isolation of the rec Mutants in Staphylococcus aureus

et al. 1972

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A histidine auxotroph (his-) of Staphylococcus aureus MS3937 and mutants sensitive to ultraviolet (UV) irradiation were obtained. The UV-sensitive mutants were found also to be sensitive to N-methyl-N'-nitro-N-nitrosoguanidine and mitomycin C, and their sensitivity was accounted for by a defect in deoxyribonucleic acid repair. Transduction of either chromosomal or plasmid markers to UV-sensitive mutants showed that these staphylococcus mutants are of the recA (reckless) type mutants as reported in Escherichia coli and Salmonella typhimurium; therefore the UV-sensitive mutants (uvri) were renamed recombination-deficient mutants (rec I. The biochemical and genetic properties of these mutants are described, and their usefulness for studies of staphylococcal plasmids is discussed.on July 31, 2020 by guest

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supporting

confidence: 62%

“…UV-sensitive mutants were obtained by a slight modification of the method described by Setlow et al (22). An overnight culture of S. aureus MS3937-1 was diluted 100-fold with fresh broth and incubated with shaking at 37 C. After incubation for 3 hr, 5 ml of this culture was suspended in 5 ml of broth containing 200 gg of NG/ml.…”

mentioning

confidence: 99%

Isolation of the rec Mutants in Staphylococcus aureus

et al. 1972

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“…The bacterial strains, bacteriophage and plasmids used in this study are listed in Table 1 (Setlow et al, 1968;Tabor and Richardson, 1985;Kunkel et al, 1987;Tomb et al, 1989;. H. influenzae strains were grown as described previously (Anderson et al, 1972).…”

Section: Bacterial Strains Bacteriophage and Plasmidsmentioning

confidence: 99%

Structural determinants of processing and secretion of the Haemophilus influenzae Hap protein

Hendrixson

Morena

Stathopoulos

et al. 1997

Molecular Microbiology

102

138

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SummaryHaemophilus influenzae elaborates a surface protein called Hap, which is associated with the capacity for intimate interaction with cultured epithelial cells. Expression of hap results in the production of three protein species: outer membrane proteins of approximately 155 kDa and 45 kDa and an extracellular protein of approximately 110 kDa. The 155 kDa protein corresponds to full-length mature Hap (without the signal sequence), and the 110 kDa extracellular protein represents the N-terminal portion of mature Hap (designated Hap s ). In the present study, we examined the mechanism of processing and secretion of Hap. Site-directed mutagenesis suggested that Hap is a serine protease that undergoes autoproteolytic cleavage to generate the 110 kDa extracellular protein and the 45 kDa outer membrane protein. Biochemical analysis confirmed this conclusion and established that cleavage occurs on the bacterial cell surface. Determination of N-terminal amino acid sequence and mutagenesis studies revealed that the 45 kDa protein corresponds to the Cterminal portion of Hap, starting at N1037. Analysis of the secondary structure of this protein (designated Hap ␤ ) predicted formation of a ␤-barrel with an N-terminal transmembrane ␣-helix followed by 14 transmembrane ␤-strands. Additional analysis revealed that the final ␤-strand contains an amino acid motif common to other ␤-barrel outer membrane proteins. Upon deletion of this entire C-terminal consensus motif, Hap could no longer be detected in the outer membrane, and secretion of Hap s was abolished. Deletion or complete alteration of the final three amino acid residues had a similar but less dramatic effect, suggesting that this terminal tripeptide is particularly important for outer membrane localization and/or stability of the protein. In contrast, isolated point mutations that disrupted the amphipathic nature of the consensus motif or eliminated the C-terminal tryptophan had no effect on outer membrane localization of Hap or secretion of Hap s . These results provide insight into a growing family of Gram-negative bacterial exoproteins that are secreted by an IgA1 protease-like mechanism; in addition, they contribute to a better understanding of the structural determinants of targeting of ␤-barrel proteins to the bacterial outer membrane.

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“…been in the laboratory for over 40 years (Alexander and Leidy, 1951); DB117 was obtained from G. Barcak (University of Maryland) (Setlow et at., 1968), H. inftuenzae strain 12 is the non-typable strain from which the genes encoding the HMW1 and HMW2 proteins were cloned (Barenkamp and Leininger, 1992); HMW1 and HMW2 are the prototyptc members of a family of non-typable Haemcphilus antigenically related high-molecular-weight adhesive proteins (St. Geme efa/., 1993).…”

Section: Discussionmentioning

confidence: 99%

A Haemophilus influenzae IgA protease‐like protein promotes intimate interaction with human epithelial cells

Falkow

1994

Molecular Microbiology

144

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Haemophilus influenzae represents a common cause of human disease and an important source of morbidity and mortality. Disease caused by this organism begins with colonization of the upper respiratory tract. Several studies indicate that H. influenzae is capable of binding to and entering cultured human cells, properties which are potentially of relevance to the process of colonization. In the present study, we isolated an H. influenzae gene designated hap, which is associated with the capacity for in vitro attachment and entry. Analysis of the derived amino acid sequence of hap demonstrated significant homology with the serine-type IgA1 proteases expressed by H. influenzae and Neisseria gonorrhoeae. It is notable that the hap product shares the catalytic domain of the IgA1 proteases and appears to be processed and secreted in an analogous manner. We speculate that the hap gene product is an important determinant of colonization, perhaps enabling the organism to evade the local immune response and thereby persist within the respiratory tract.

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Repair of Deoxyribonucleic Acid in Haemophilus influenzae I. X-Ray Sensitivity of Ultraviolet-sensitive Mutants and Their Behavior as Hosts to Ultraviolet-irradiated Bacteriophage and Transforming Deoxyribonucleic Acid

Cited by 180 publications

References 16 publications

Isolation of the rec Mutants in Staphylococcus aureus

Isolation of the rec Mutants in Staphylococcus aureus

Structural determinants of processing and secretion of the Haemophilus influenzae Hap protein

A Haemophilus influenzae IgA protease‐like protein promotes intimate interaction with human epithelial cells

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