scholarly journals Ehrlichia chaffeensis TRP120 nucleomodulin binds DNA with disordered tandem repeat domain

PLoS ONE ◽  
2018 ◽  
Vol 13 (4) ◽  
pp. e0194891 ◽  
Author(s):  
Valerie J. Klema ◽  
Krishna Mohan Sepuru ◽  
Nadia Füllbrunn ◽  
Tierra R. Farris ◽  
Paige S. Dunphy ◽  
...  
Keyword(s):  
Tandem Repeat ◽  
Ehrlichia Chaffeensis ◽  
Repeat Domain

scholarly journals The MUC1 Cytoplasmic Tail and Tandem Repeat Domains Contribute to Mammary Oncogenesis in FVB Mice

2008 ◽  
Vol 1 ◽  
pp. BCBCR.S655
Author(s):  
Christine L. Hattrup ◽  
Judy M. Bradley ◽  
Kari L. Kotlarczyk ◽  
Cathy S. Madsen ◽  
Joseph G. Hentz ◽  
...  
Keyword(s):  
Mouse Models ◽  
Tandem Repeat ◽  
Late Onset ◽  
Cytoplasmic Tail ◽  
Mammary Carcinogenesis ◽  
Tumor Formation ◽  
Full Length ◽  
Relative Importance ◽  
Cancer Model ◽  
Repeat Domain

Background Though the importance of the transmembrane mucin MUC1 in mammary oncogenesis has long been recognized, the relative contributions of the cytoplasmic tail and tandem repeat domains are poorly understood. Methods To address this, mouse models of mammary carcinogenesis were created expressing full-length cytoplasmic tail-deleted, or tandem repeat-deleted MUC1 constructs. Results Overexpression of full-length MUC1 resulted in tumor formation in young mice (≤ 12 months); however, loss of either the cytoplasmic tail or the tandem repeat domain abrogated this oncogenic capacity. Aged mice in all strains developed late-onset mammary tumors similar to those previously described for the FVB background. Conclusions This study is the first spontaneous cancer model to address the relative importance of the cytoplasmic tail and tandem repeat domains to MUC1-driven mammary oncogenesis, and suggests that both of these domains are essential for tumor formation.

Primary structure of the variable regions of a monoclonal antibody MUSE11 recognizing the tandem repeat domain of a mucin core protein, MUC1

1993 ◽  
Vol 7 (2) ◽  
pp. 100-104 ◽  
Author(s):  
Yuji Hinoda ◽  
Yoshiaki Arimura ◽  
Fumio Itoh ◽  
Masaaki Adachi ◽  
Masayuki Tsujisaki ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Tandem Repeat ◽  
Primary Structure ◽  
Core Protein ◽  
Variable Regions ◽  
Repeat Domain ◽  
Mucin Core Protein

scholarly journals Human mucin gene MUC4: organization of its 5′-region and polymorphism of its central tandem repeat array

1998 ◽  
Vol 332 (3) ◽  
pp. 739-748 ◽  
Author(s):  
Séverine NOLLET ◽  
Nicolas MONIAUX ◽  
Jacques MAURY ◽  
Danièle PETITPREZ ◽  
Pierre DEGAND ◽  
...  
Keyword(s):  
Signal Peptide ◽  
Tandem Repeat ◽  
Tandem Repeats ◽  
Cysteine Residue ◽  
Coding Region ◽  
Exon 2 ◽  
Repeat Array ◽  
Mucin Gene ◽  
Repeat Domain ◽  
Tandem Repeat Array

In a previous study we isolated a partial cDNA with a tandem repeat of 48 bp, which allowed us to map a novel human mucin gene named MUC4to chromosome 3q29. Here we report the organization and sequence of the 5´-region and its junction with the tandem repeat array of MUC4. Analysis of three overlapping genomic clones allowed us to obtain a partial restriction map of MUC4 and to locate the complete 48 bp tandem repeat domain on a PstI/EcoRI genomic fragment that exhibits a very large variation in number of tandem repeats (7–19 kb). cDNA clonal extension allowed us to obtain the entire 5´ coding region of MUC4. Exon 1 consists of a 5´ untranslated region and an 82 bp fragment encoding the signal peptide. This latter shows a high degree of similarity to the signal peptide of another apomucin, ASGP-1. Exon 2 is extremely large and contains a unique sequence that is followed by the whole tandem repeat domain. It encodes only one cysteine residue, making MUC4 different from mucin genes belonging to the 11p15.5 family. Moreover, an intron downstream from the tandem repeat array consists mainly of a 15 bp tandem repeat that exhibits a polymorphism in having a variable number of tandem repeats.

scholarly journals Ehrlichia chaffeensis TRP120 Binds a G+C-Rich Motif in Host Cell DNA and Exhibits Eukaryotic Transcriptional Activator Function

2011 ◽  
Vol 79 (11) ◽  
pp. 4370-4381 ◽  
Author(s):  
Bing Zhu ◽  
Jeeba A. Kuriakose ◽  
Tian Luo ◽  
Efren Ballesteros ◽  
Sharu Gupta ◽  
...  
Keyword(s):  
Transcriptional Regulation ◽  
Dna Binding ◽  
Host Cell ◽  
High Throughput ◽  
Tandem Repeat ◽  
Binding Sites ◽  
Host Gene ◽  
Host Cells ◽  
Ehrlichia Chaffeensis ◽  
Content Type

ABSTRACTEhrlichia chaffeensisis an obligately intracellular bacterium that modulates host cell gene transcription in the mononuclear phagocyte, but the host gene targets and mechanisms involved in transcriptional modulation are not well-defined. In this study, we identified a novel tandem repeat DNA-binding domain in theE. chaffeensis120-kDa tandem repeat protein (TRP120) that directly binds host cell DNA. TRP120 was observed by immunofluorescent microscopy in the nucleus ofE. chaffeensis-infected host cells and was detected in nuclear extracts by Western immunoblotting with TRP120-specific antibody. The TRP120 binding sites and associated host cell target genes were identified using high-throughput deep sequencing (Illumina) of immunoprecipitated DNA (chromatin immunoprecipitation and high-throughput DNA sequencing). Multiple em motif elicitation (MEME) analysis of the most highly enriched TRP120-bound sequences revealed a G+C-rich DNA motif, and recombinant TRP120 specifically bound synthetic oligonucleotides containing the motif. TRP120 target gene binding sites were mapped most frequently to intersecting regions (intron/exon; 49%) but were also identified in upstream regulatory regions (25%) and downstream locations (26%). Genes targeted by TRP120 were most frequently associated with transcriptional regulation, signal transduction, and apoptosis. TRP120 targeted inflammatory chemokine genes, CCL2, CCL20, and CXCL11, which were strongly upregulated duringE. chaffeensisinfection and were also upregulated by direct transfection with recombinant TRP120. This study reveals that TRP120 is a novel DNA-binding protein that is involved in a host gene transcriptional regulation strategy.

scholarly journals 1P083 STPR, a 23-amino-acid tandem repeat domain, found in the human function-unknown protein ZNF821(Protein:Function,The 48th Annual Meeting of the Biophysical Society of Japan)

2010 ◽  
Vol 50 (supplement2) ◽  
pp. S33-S34
Author(s):  
Etsuro OKABE ◽  
Yasuhiro NONAKA ◽  
Hideki MUTO ◽  
Tomoyasu AIZAWA ◽  
Shohei MYOBA ◽  
...  
Keyword(s):  
Amino Acid ◽  
Annual Meeting ◽  
Tandem Repeat ◽  
Unknown Protein ◽  
Repeat Domain ◽  
Biophysical Society ◽  
Human Function

scholarly journals Tyrosine-Phosphorylated Ehrlichia chaffeensis and Ehrlichia canis Tandem Repeat Orthologs Contain a Major Continuous Cross-Reactive Antibody Epitope in Lysine-Rich Repeats

2011 ◽  
Vol 79 (8) ◽  
pp. 3178-3187 ◽  
Author(s):  
Jere W. McBride ◽  
Xiaofeng Zhang ◽  
Abdul Wakeel ◽  
Jeeba A. Kuriakose
Keyword(s):  
Amino Acids ◽  
Tandem Repeat ◽  
Tandem Repeats ◽  
Ehrlichia Canis ◽  
Small Subset ◽  
Ehrlichia Chaffeensis ◽  
Whole Cell ◽  
Content Type ◽  
Cell Lysates ◽  
Species Specific

ABSTRACTA small subset of major immunoreactive proteins have been identified inEhrlichia chaffeensisandEhrlichia canis, including three molecularly and immunologically characterized pairs of immunoreactive tandem repeat protein (TRP) orthologs with major continuous species-specific epitopes within acidic tandem repeats (TR) that stimulate strong antibody responses during infection. In this study, we identified a fourth major immunoreactive TR-containing ortholog pair and defined a major cross-reactive epitope in homologous nonidentical 24-amino-acid lysine-rich TRs. Antibodies from patients and dogs with ehrlichiosis reacted strongly with recombinant TR regions, and epitopes were mapped to the N-terminal TR region (18 amino acids) inE. chaffeensisand the complete TR (24 amino acids) inE. canis. Two less-dominant epitopes were mapped to adjacent glutamate/aspartate-rich and aspartate/tyrosine-rich regions in the acidic C terminus ofE. canisTRP95 but not inE. chaffeensisTRP75. Major immunoreactive proteins inE. chaffeensis(75-kDa) andE. canis(95-kD) whole-cell lysates and supernatants were identified with TR-specific antibodies. Consistent with other ehrlichial TRPs, the TRPs identified in ehrlichial whole-cell lysates and the recombinant proteins migrated abnormally slow electrophoretically a characteristic that was demonstrated with the positively charged TR and negatively charged C-terminal domains.E. chaffeensisTRP75 andE. canisTRP95 were immunoprecipitated with anti-pTyr antibody, demonstrating that they are tyrosine phosphorylated during infection of the host cell.

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