Nucleotide and deduced amino acid sequences of the lacR, lacABCD, and lacFE genes encoding the repressor, tagatose 6-phosphate gene cluster, and sugar-specific phosphotransferase system components of the lactose operon of Streptococcus mutans.

ABSTRACT Intracellular polysaccharides (IPS) are glycogen-like storage polymers which contribute significantly to Streptococcus mutans-induced cariogenesis. We previously identified and cloned a locus from the S. mutans chromosome which is required for the accumulation of IPS. Sequencing of this locus revealed at least four contiguous open reading frames, all of which are preceded by a common promoter region and are transcribed in the same direction. Analysis of the amino acid sequence deduced from the first of these open reading frames (ORF1) revealed domains which are highly conserved among d-alanine-activating enzymes (DltA) inLactobacillus rhamnosus (formerlyLactobacillus casei) and Bacillus subtilis. The deduced amino acid sequences derived from ORF2, -3, and -4 also exhibit extensive similarity to DltB, -C, and -D, respectively, in these microorganisms. However, Southern hybridization experiments indicate that this operon maps to a locus on the S. mutanschromosome which is separate from the glgP,glgA, and glgD genes, whose products are known mediators of bacterial IPS accumulation. We therefore assigned a newdlt designation to the locus which we had formerly calledglg. We maintain that the dlt genes are involved in S. mutans IPS accumulation, however, since they complement a mutation in trans which otherwise rendersS. mutans IPS deficient. In this study, we found that expression of the S. mutans dlt genes is growth phase dependent and is modulated by carbohydrates internalized via the phosphoenolpyruvate phosphotransferase system (PTS). We demonstrated that the S. mutans dlt genes are expressed constitutively when non-PTS sugars are provided as the sole source of carbohydrate. Consistent with a role for the PTS in dltexpression is a similar constitutive expression of the dltgenes in an S. mutans PTS mutant grown in a chemically defined medium supplemented with glucose. In summary, these findings support a novel role for the dlt gene products inS. mutans IPS accumulation and suggest thatdlt expression in this oral pathogen is subject to complex mechanisms of control imposed by growth phase, dietary carbohydrate, and other factors present in the plaque environment.

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Structural and antigenic polymorphism of the 35- to 48-kilodalton merozoite surface antigen (MSA-2) of the malaria parasite Plasmodium falciparum

Molecular and Cellular Biology ◽

10.1128/mcb.11.2.963-971.1991 ◽

1991 ◽

Vol 11 (2) ◽

pp. 963-971

Author(s):

B Fenton ◽

J T Clark ◽

C M Khan ◽

J V Robinson ◽

D Walliker ◽

...

Keyword(s):

Plasmodium Falciparum ◽

Amino Acid ◽

Surface Antigen ◽

Dna Sequences ◽

Amino Acid Sequences ◽

Merozoite Surface Antigen ◽

Parasite Plasmodium ◽

Genes Encoding ◽

Parasite Plasmodium Falciparum ◽

Group B

Merozoite surface antigen MSA-2 of the human parasite Plasmodium falciparum is being considered for the development of a malaria vaccine. The antigen is polymorphic, and specific monoclonal antibodies differentiate five serological variants of MSA-2 among 25 parasite isolates. The variants are grouped into two major serogroups, A and B. Genes encoding two different variants from serogroup A have been sequenced, and their DNA together with deduced amino acid sequences were compared with sequences encoded by other alleles. The comparison shows that the serological classification reflects differences in DNA sequences and deduced primary structure of MSA-2 variants and serogroups. Thus, the overall homologies of DNA and amino acid sequences are over 95% among variants in the same serogroup. In contrast, similarities between the group A variants and a group B variant are only 70 and 64% for DNA and amino acid sequences, respectively. We propose that the MSA-2 protein is encoded by two highly divergent groups of alleles, with limited additional polymorphism displayed within each group.

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The Biopesticide Paenibacillus popilliae Has a Vancomycin Resistance Gene Cluster Homologous to the Enterococcal VanA Vancomycin Resistance Gene Cluster

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.44.3.705-709.2000 ◽

2000 ◽

Vol 44 (3) ◽

pp. 705-709 ◽

Cited By ~ 60

Author(s):

Robin Patel ◽

Kerryl Piper ◽

Franklin R. Cockerill ◽

James M. Steckelberg ◽

Allan A. Yousten

Keyword(s):

Gene Cluster ◽

Resistance Gene ◽

Bacterial Resistance ◽

Vancomycin Resistance ◽

Amino Acid Sequences ◽

Agricultural Practice ◽

Human Pathogens ◽

Resistance Gene Cluster ◽

Genes Encoding ◽

Vancomycin Resistant

ABSTRACT We have previously identified, in Paenibacillus popilliae, a 708-bp sequence which has homology to the sequence of the enterococcal vanA gene. We have performed further studies revealing five genes encoding homologues of VanY, VanZ, VanH, VanA, and VanX in P. popilliae. The predicted amino acid sequences are similar to those in VanA vancomycin-resistant enterococci: 61% identity for VanY, 21% for VanZ, 74% for VanH, 77% for VanA, and 79% for VanX. The genes in P. popilliae may have been a precursor to or have had ancestral genes in common with vancomycin resistance genes in enterococci. The use of P. popilliae biopesticidal preparations in agricultural practice may have an impact on bacterial resistance in human pathogens.

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Genes for low-molecular-weight heat shock proteins of soybeans: sequence analysis of a multigene family.

Molecular and Cellular Biology ◽

10.1128/mcb.5.12.3417 ◽

1985 ◽

Vol 5 (12) ◽

pp. 3417-3428 ◽

Cited By ~ 65

Author(s):

R T Nagao ◽

E Czarnecka ◽

W B Gurley ◽

F Schöffl ◽

J L Key

Keyword(s):

Molecular Weight ◽

Amino Acid ◽

Heat Shock ◽

Dna Sequences ◽

Regulatory Element ◽

Amino Acid Sequences ◽

Striking Similarity ◽

Low Molecular Weight ◽

Genes Encoding ◽

Flanking Regions

Soybeans, Glycine max, synthesize a family of low-molecular-weight heat shock (HS) proteins in response to HS. The DNA sequences of two genes encoding 17.5- and 17.6-kilodalton HS proteins were determined. Nuclease S1 mapping of the corresponding mRNA indicated multiple start termini at the 5' end and multiple stop termini at the 3' end. These two genes were compared with two other soybean HS genes of similar size. A comparison among the 5' flanking regions encompassing the presumptive HS promoter of the soybean HS-protein genes demonstrated this region to be extremely homologous. Analysis of the DNA sequences in the 5' flanking regions of the soybean genes with the corresponding regions of Drosophila melanogaster HS-protein genes revealed striking similarity between plants and animals in the presumptive promoter structure of thermoinducible genes. Sequences related to the Drosophila HS consensus regulatory element were found 57 to 62 base pairs 5' to the start of transcription in addition to secondary HS consensus elements located further upstream. Comparative analysis of the deduced amino acid sequences of four soybean HS proteins illustrated that these proteins were greater than 90% homologous. Comparison of the amino acid sequence for soybean HS proteins with other organisms showed much lower homology (less than 20%). Hydropathy profiles for Drosophila, Xenopus, Caenorhabditis elegans, and G. max HS proteins showed a similarity of major hydrophilic and hydrophobic regions, which suggests conservation of functional domains for these proteins among widely dispersed organisms.

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The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits

Biochemical Journal ◽

10.1042/bj3170187 ◽

1996 ◽

Vol 317 (1) ◽

pp. 187-194 ◽

Cited By ~ 55

Author(s):

Stanislaw ZOLNIEROWICZ ◽

Christine VAN HOOF ◽

Nataša ANDJELKOVIĆ ◽

Peter CRON ◽

Ilse STEVENS ◽

...

Keyword(s):

Amino Acid ◽

Protein Phosphatase ◽

Amino Acid Sequences ◽

Regulatory Subunits ◽

Consensus Sequences ◽

Reverse Transcription Pcr ◽

Genes Encoding ◽

Phosphatase 2A ◽

Molecular Masses ◽

Specific Mrnas

Two protein phosphatase 2A (PP2A) holoenzymes were isolated from rabbit skeletal muscle containing, in addition to the catalytic and PR65 regulatory subunits, proteins of apparent molecular masses of 61 and 56 kDa respectively. Both holoenzymes displayed low basal phosphorylase phosphatase activity, which could be stimulated by protamine to an extent similar to that of previously characterized PP2A holoenzymes. Protein microsequencing of tryptic peptides derived from the 61 kDa protein, termed PR61, yielded 117 residues of amino acid sequence. Molecular cloning by enrichment of specific mRNAs, followed by reverse transcription–PCR and cDNA library screening, revealed that this protein exists in multiple isoforms encoded by at least three genes, one of which gives rise to several splicing variants. Comparisons of these sequences with the available databases identified one more human gene and predicted another based on a rabbit cDNA-derived sequence, thus bringing the number of genes encoding PR61 family members to five. Peptide sequences derived from PR61 corresponded to the deduced amino acid sequences of either α or β isoforms, indicating that the purified PP2A preparation was a mixture of at least two trimers. In contrast, the 56 kDa subunit (termed PR56) seems to correspond to the ϵ isoform of PR61. Several regulatory subunits of PP2A belonging to the PR61 family contain consensus sequences for nuclear localization and might therefore target PP2A to nuclear substrates.

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Structural and antigenic polymorphism of the 35- to 48-kilodalton merozoite surface antigen (MSA-2) of the malaria parasite Plasmodium falciparum.

Molecular and Cellular Biology ◽

10.1128/mcb.11.2.963 ◽

1991 ◽

Vol 11 (2) ◽

pp. 963-971 ◽

Cited By ~ 98

Author(s):

B Fenton ◽

J T Clark ◽

C M Khan ◽

J V Robinson ◽

D Walliker ◽

...

Keyword(s):

Plasmodium Falciparum ◽

Amino Acid ◽

Surface Antigen ◽

Dna Sequences ◽

Amino Acid Sequences ◽

Merozoite Surface Antigen ◽

Parasite Plasmodium ◽

Genes Encoding ◽

Parasite Plasmodium Falciparum ◽

Group B

Merozoite surface antigen MSA-2 of the human parasite Plasmodium falciparum is being considered for the development of a malaria vaccine. The antigen is polymorphic, and specific monoclonal antibodies differentiate five serological variants of MSA-2 among 25 parasite isolates. The variants are grouped into two major serogroups, A and B. Genes encoding two different variants from serogroup A have been sequenced, and their DNA together with deduced amino acid sequences were compared with sequences encoded by other alleles. The comparison shows that the serological classification reflects differences in DNA sequences and deduced primary structure of MSA-2 variants and serogroups. Thus, the overall homologies of DNA and amino acid sequences are over 95% among variants in the same serogroup. In contrast, similarities between the group A variants and a group B variant are only 70 and 64% for DNA and amino acid sequences, respectively. We propose that the MSA-2 protein is encoded by two highly divergent groups of alleles, with limited additional polymorphism displayed within each group.

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Characterization of Novel Carbazole Catabolism Genes from Gram-Positive Carbazole Degrader Nocardioides aromaticivorans IC177

Applied and Environmental Microbiology ◽

10.1128/aem.72.5.3321-3329.2006 ◽

2006 ◽

Vol 72 (5) ◽

pp. 3321-3329 ◽

Cited By ~ 40

Author(s):

Kengo Inoue ◽

Hiroshi Habe ◽

Hisakazu Yamane ◽

Hideaki Nojiri

Keyword(s):

Amino Acid ◽

Gene Clusters ◽

Amino Acid Sequences ◽

Open Reading Frames ◽

Class Iii ◽

Rt Pcr ◽

Gram Positive ◽

Mononuclear Iron ◽

Reverse Transcription Pcr ◽

Genes Encoding

ABSTRACT Nocardioides aromaticivorans IC177 is a gram-positive carbazole degrader. The genes encoding carbazole degradation (car genes) were cloned into a cosmid clone and sequenced partially to reveal 19 open reading frames. The car genes were clustered into the carAaCBaBbAcAd and carDFE gene clusters, encoding the enzymes responsible for the degradation of carbazole to anthranilate and 2-hydroxypenta-2,4-dienoate and of 2-hydroxypenta-2,4-dienoate to pyruvic acid and acetyl coenzyme A, respectively. The conserved amino acid motifs proposed to bind the Rieske-type [2Fe-2S] cluster and mononuclear iron, the Rieske-type [2Fe-2S] cluster, and flavin adenine dinucleotide were found in the deduced amino acid sequences of carAa, carAc, and carAd, respectively, which showed similarities with CarAa from Sphingomonas sp. strain KA1 (49% identity), CarAc from Pseudomonas resinovorans CA10 (31% identity), and AhdA4 from Sphingomonas sp. strain P2 (37% identity), respectively. Escherichia coli cells expressing CarAaAcAd exhibited major carbazole 1,9a-dioxygenase (CARDO) activity. These data showed that the IC177 CARDO is classified into class IIB, while gram-negative CARDOs are classified into class III or IIA, indicating that the respective CARDOs have diverse types of electron transfer components and high similarities of the terminal oxygenase. Reverse transcription-PCR (RT-PCR) experiments showed that the carAaCBaBbAcAd and carDFE gene clusters are operonic. The results of quantitative RT-PCR experiments indicated that transcription of both operons is induced by carbazole or its metabolite, whereas anthranilate is not an inducer. Biotransformation analysis showed that the IC177 CARDO exhibits significant activities for naphthalene, carbazole, and dibenzo-p-dioxin but less activity for dibenzofuran and biphenyl.

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Nucleotide and deduced amino acid sequences of genes encoding the structural and nonstructural NS1 proteins of a dengue-2 virus isolated in China

Virus Genes ◽

10.1007/bf01703603 ◽

1994 ◽

Vol 8 (1) ◽

pp. 71-74 ◽

Cited By ~ 3

Author(s):

Pei-Ying Yang ◽

Ingrid Kautner ◽

Chong-Lek Koh ◽

Sai-Kit Lam

Keyword(s):

Amino Acid ◽

Amino Acid Sequences ◽

Genes Encoding

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Detection of Polymorphisms in the Human Urokinase-type Plasminogen Activator Gene

Thrombosis and Haemostasis ◽

10.1055/s-0038-1655983 ◽

1997 ◽

Vol 77 (03) ◽

pp. 434-435 ◽

Cited By ~ 11

Author(s):

B Conne ◽

M Berczy ◽

D Belin

Keyword(s):

Amino Acid ◽

Plasminogen Activator ◽

Tumor Metastasis ◽

Amino Acid Sequences ◽

Kringle Domain ◽

Type Plasminogen Activator ◽

Urokinase Type Plasminogen Activator ◽

Genes Encoding

SummaryExpressed polymorphisms in the genes encoding components of the fibrinolytic cascade could have implications for the predisposition to thrombolytic disorders and/or for tumor metastasis. The occurrence of published two amino acid sequences at position 194 of the human urokinase-type plasminogen activator prompted us to search by SSCP for frequent polymorphisms in several exons of the gene. Surprisingly, only one sequence was detected in codon 194 (>200 alleles). Two polymorphisms were observed in this study: the most frequent one, a C to T change near the beginning of exon 8, is probably silent; a less frequent polymorphism results in the replacement of a Leu residue by a Pro, in the kringle domain.

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Sequences of beta-lactamase genes encoding CTX-M-1 (MEN-1) and CTX-M-2 and relationship of their amino acid sequences with those of other beta-lactamases.

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.40.2.509 ◽

1996 ◽

Vol 40 (2) ◽

pp. 509-513 ◽

Cited By ~ 133

Author(s):

A Bauernfeind ◽

I Stemplinger ◽

R Jungwirth ◽

S Ernst ◽

J M Casellas

Keyword(s):

Amino Acid ◽

Klebsiella Oxytoca ◽

Amino Acid Sequences ◽

Protein Sequencing ◽

Beta Lactamase ◽

Beta Lactamases ◽

Class A ◽

Men 1 ◽

Genes Encoding ◽

Relationship Of

Amino acid sequences determined either by protein sequencing or by DNA sequencing are identical for cefotaximases CTX-M-1 and MEN-1, whereas CTX-M-2 is 84% identical to CTX-M-1/MEN-1. Both beta-lactamases are distantly related to other plasmidic class A enzymes (homology to TEM-1 is 38.1% for CTX-M-1/MEN-1 and 36.5% for CTX-M-2); the closest relationship was with the chromosomal beta-lactamase of Klebsiella oxytoca E23004 (homologies of 74.5% for CTX-M-1/MEN-1 and 77.9% for CTX-M-2). The cefotaximases CTX-M-1/MEN-1 and CTX-M-2 represent two members of a new subgroup of plasmidic class A beta-lactamases.

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