Reproducible and variable rearrangements of a Tetrahymena thermophila surface protein gene family occur during macronuclear development

1988 ◽  
Vol 8 (11) ◽  
pp. 5043-5046
Author(s):  
J P Kile ◽  
H D Love ◽  
C A Hubach ◽  
G A Bannon
Keyword(s):  
Environmental Regulation ◽  
Cdna Clone ◽  
Multigene Family ◽  
Protein Gene ◽  
Tetrahymena Thermophila ◽  
Surface Protein ◽  
Surface Proteins ◽  
Hybridization Probe ◽  
Macronuclear Development ◽  
Surface Protein Gene

The expression of Tetrahymena surface proteins serotype H3 (SerH3) and serotype T (SerT) is under environmental regulation. SerH3 is expressed when cells are incubated between the temperatures of 20 and 35 degrees C, while SerT is expressed when cells are grown at temperatures above 35 degrees C. Using a SerH3 cDNA clone as a hybridization probe, we determined that (i) the SerH3 gene is a member of a multigene family; (ii) most members of this multigene family are variably rearranged during macronuclear development; and (iii) the gene which produces the SerH3 mRNA is reproducibly rearranged during macronuclear development.

scholarly journals Reproducible and variable rearrangements of a Tetrahymena thermophila surface protein gene family occur during macronuclear development.

1988 ◽  
Vol 8 (11) ◽  
pp. 5043-5046 ◽  
Author(s):  
J P Kile ◽  
H D Love ◽  
C A Hubach ◽  
G A Bannon
Keyword(s):  
Environmental Regulation ◽  
Cdna Clone ◽  
Multigene Family ◽  
Protein Gene ◽  
Tetrahymena Thermophila ◽  
Surface Protein ◽  
Surface Proteins ◽  
Hybridization Probe ◽  
Macronuclear Development ◽  
Surface Protein Gene

The expression of Tetrahymena surface proteins serotype H3 (SerH3) and serotype T (SerT) is under environmental regulation. SerH3 is expressed when cells are incubated between the temperatures of 20 and 35 degrees C, while SerT is expressed when cells are grown at temperatures above 35 degrees C. Using a SerH3 cDNA clone as a hybridization probe, we determined that (i) the SerH3 gene is a member of a multigene family; (ii) most members of this multigene family are variably rearranged during macronuclear development; and (iii) the gene which produces the SerH3 mRNA is reproducibly rearranged during macronuclear development.

High Frequency Intragenic Recombination During Macronuclear Development in Tetrahymena thermophila Restores the Wild-type SerH1 Gene

Genetics ◽  
1998 ◽  
Vol 148 (3) ◽  
pp. 1109-1115
Author(s):  
J C Deak ◽  
F P Doerder
Keyword(s):  
High Frequency ◽  
Tetrahymena Thermophila ◽  
Genetic Material ◽  
Surface Protein ◽  
Intragenic Recombination ◽  
Wild Type ◽  
Macronuclear Development ◽  
Surface Protein Gene ◽  
In Trans ◽  
Mitosis And Meiosis

Abstract Macronuclear development in ciliates is characterized by extensive rearrangement of genetic material, including sequence elimination, chromosome fragmentation and telomere addition. Intragenic recombination is a relatively rare, but evolutionarily important phenomenon occurring in mitosis and meiosis in a wide variety of organisms. Here, we show that high frequency intragenic recombination, on the order of 30%, occurs in the developing amitotic macronucleus of the ciliate Tetrahymena thermophila. Such recombination, occurring between two nonsense transition mutations separated by 726 nucleotides, reproducibly restores wild-type expression of the SerH1 surface protein gene, thus mimicking complementation in trans heterozygotes. Recombination must be considered a potentially important aspect of macronuclear development, producing gene combinations not present in the germinal micronucleus.

Serotype and surface protein gene distribution of colonizing group B streptococcus in women in Egypt

2013 ◽  
Vol 142 (1) ◽  
pp. 208-210 ◽  
Author(s):  
S. SHABAYEK ◽  
S. ABDALLA ◽  
A. MH. ABOUZEID
Keyword(s):  
High Frequency ◽  
Protein Gene ◽  
Group B Streptococcus ◽  
Surface Protein ◽  
Surface Proteins ◽  
Protein Encoding ◽  
Vaginal Swabs ◽  
Surface Protein Gene ◽  
Group B ◽  
Encoding Genes

SUMMARYGroup B streptococcus (GBS) is a leading cause of neonatal sepsis and meningitis. We determined the distribution of serotypes and surface protein encoding genes of GBS strains from pregnant and non-pregnant women in Egypt. Vaginal swabs from 364 women were screened by culture and 100 (27·4%) yielded GBS. Serotype V was the most predominant (33%), followed by serotypes II (17%), III (15%), Ia (14%), VI (12%), Ib (8%) and IV (1%). The most common surface protein genes were epsilon (27%), alp3 (26%), bca (18%), rib (16%) and alp2 (10%). Two isolates were negative for surface protein genes. The distribution of serotypes and surface proteins was similar to reports from other parts of the world but the relatively high frequency of serotype VI was a notable feature of the strains from women in Egypt.

Three strains of Wolbachia pipientis and high rates of infection in Iranian sandfly species

2014 ◽  
Vol 104 (2) ◽  
pp. 195-202 ◽  
Author(s):  
A. Bordbar ◽  
S. Soleimani ◽  
F. Fardid ◽  
M.R. Zolfaghari ◽  
P. Parvizi
Keyword(s):  
Protein Gene ◽  
Surface Protein ◽  
Male And Female ◽  
Wolbachia Pipientis ◽  
Major Surface Protein ◽  
Zoonotic Cutaneous Leishmaniasis ◽  
Geographical Regions ◽  
Surface Protein Gene ◽  
Major Surface ◽  
Zoonotic Visceral Leishmaniasis

AbstractIndividual wild-caught sandflies from Iran were examined for infections of Wolbachia pipientis by targeting the major surface protein gene wsp of this intracellular α-proteobacterium. In total, 638 male and female sandflies were screened, of which 241 were found to be positive for one of three wsp haplotypes. Regardless of geographical origins and habitats, Phlebotomus (Phlebotomus) papatasi and other sandfly species were found to be infected with one common, widespread strain of A-group W. pipientis (Turk 54, GenBank accession EU780683; AY288297). In addition, a new A-group haplotype (Turk07, GenBank accession KC576916) was isolated from Phlebotomus (Paraphlebotomus) mongolensis and Phlebotomus (Pa.) caucasicus, and a new B-group haplotype (AZ2331, GenBank accession JX488735) was isolated from Phlebotomus (Larroussius) perfiliewi. Therefore, Wolbachia was found to occur in at least three of the incriminated vectors of zoonotic cutaneous leishmaniasis and zoonotic visceral leishmaniasis in different geographical regions of Iran. It may provide a new tool for the future control of leishmaniasis.

Structure and expression of two temperature-specific surface proteins in the ciliated protozoan Tetrahymena thermophila

1986 ◽  
Vol 6 (9) ◽  
pp. 3240-3245
Author(s):  
G A Bannon ◽  
R Perkins-Dameron ◽  
A Allen-Nash
Keyword(s):  
Cell Surface ◽  
Specific Surface ◽  
Incubation Temperature ◽  
Tetrahymena Thermophila ◽  
Sodium Dodecyl ◽  
Surface Protein ◽  
Surface Proteins ◽  
Ciliated Protozoan ◽  
Temperature Dependent ◽  
Molecular Sizes

The presence of specific proteins (known as immobilization antigens) on the surface of the ciliated protozoan Tetrahymena thermophila is under environmental regulation. There are five different classes (serotypes) of surface proteins which appear on the cell surface when T. thermophila is cultured under different conditions of temperature or incubation medium; three of these are temperature dependent. The appearance of these proteins on the cell surface is mutually exclusive. We used polyclonal antibodies raised against 30 degrees C (designated SerH3)- and 40 degrees C (designated SerT)-specific surface antigens to study their structure and expression. We showed that these surface proteins contain at least one disulfide bridge. On sodium dodecyl sulfate-denaturing polyacrylamide gels, the nonreduced 30 degrees C- and 40 degrees C-specific surface proteins migrated with molecular sizes of 69 and 36 kilodaltons, respectively. The reduced forms of the proteins migrated with molecular sizes of 58 and 30 kilodaltons, respectively. The synthesis of the surface proteins responded rapidly and with a time course similar to that of the incubation temperature. The synthesis of each surface protein was greatly reduced within 1 h and undetectable by 2 h after a shift to the temperature at which the protein is not expressed. Surface protein synthesis resumed by the end of 1 h after a shift to the temperature at which the protein is expressed. The temperature-dependent induction of these surface proteins appears to be dependent on the synthesis of new mRNA, as indicated by a sensitivity to actinomycin D. Surface protein syntheses were mutually exclusive except at a transition temperature. At 35 degrees C both surface proteins were synthesized by a cell population. These data support the potential of this system as a model for the study of the effects of environmental factors on the genetic regulation of cell surface proteins.

scholarly journals Antigenic diversity ofTheileriamajor piroplasm surface protein gene in Jeju black cattle

2008 ◽  
Vol 9 (2) ◽  
pp. 155 ◽  
Author(s):  
Myung-Soon Ko ◽  
Kyoung-Kap Lee ◽  
Kyu-Kye Hwang ◽  
Byung-Sun Kim ◽  
Gui-Cheol Choi ◽  
...  
Keyword(s):  
Protein Gene ◽  
Surface Protein ◽  
Antigenic Diversity ◽  
Surface Protein Gene ◽  
Jeju Black Cattle

scholarly journals Enterococcal Surface Protein Esp Is Important for Biofilm Formation of Enterococcus faecium E1162

2007 ◽  
Vol 189 (22) ◽  
pp. 8233-8240 ◽  
Author(s):  
Esther Heikens ◽  
Marc J. M. Bonten ◽  
Rob J. L. Willems
Keyword(s):  
Enterococcus Faecium ◽  
Biofilm Formation ◽  
Deletion Mutant ◽  
Wild Type Strain ◽  
Protein Gene ◽  
Surface Protein ◽  
Essential Factor ◽  
Wild Type ◽  
Surface Protein Gene ◽  
Multiple Antibiotics

ABSTRACT Enterococci have emerged as important nosocomial pathogens with resistance to multiple antibiotics. Adhesion to abiotic materials and biofilm formation on medical devices are considered important virulence properties. A single clonal lineage of Enterococcus faecium, complex 17 (CC17), appears to be a successful nosocomial pathogen, and most CC17 isolates harbor the enterococcal surface protein gene, esp. In this study, we constructed an esp insertion-deletion mutant in a clinical E. faecium CC17 isolate. In addition, initial adherence and biofilm assays were performed. Compared to the wild-type strain, the esp insertion-deletion mutant no longer produced Esp on the cell surface and had significantly lower initial adherence to polystyrene and significantly less biofilm formation, resulting in levels of biofilm comparable to those of an esp-negative isolate. Capacities for initial adherence and biofilm formation were restored in the insertion-deletion mutant by in trans complementation with esp. These results identify Esp as the first documented determinant in E. faecium CC17 with an important role in biofilm formation, which is an essential factor in infection pathogenesis.

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