TITLE

Genomic Structure and Characterization of the Drosophila S3 Ribosomal/DNA Repair Gene and Mutant Alleles

AUTHOR(S)
Kelley, M.R.; Wilson III, D.M.; Deutsch, W.A.
PUB. DATE
March 2000
SOURCE
DNA & Cell Biology;Mar2000, Vol. 19 Issue 3, p149
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
The Drosophila S3 protein is known to be associated with ribosomes, where it is thought to play a role in the initiation of protein translation. The S3 protein also contains a DNA repair activity, efficiently processing 8- oxoguanine residues in DNA via an N-glycosylase/apurinic-apyrimidinic (AP) lyase activity. The gene that encodes S3 has previously been localized to one of the Minute loci on chromosome 3 in Drosophila. This study focused on the genomic organization of S3 at M(3)95A, initial promoter characterization, and analysis of three mutant alleles at this locus. The S3 gene was found to be a single-copy gene 2 to 3 kb in length and containing a single intron. The upstream 1.6-kb region was analyzed for promoter activity, identifying a presumptive regulatory domain containing potential enhancer and suppressor elements. This finding is of interest, as the S3 gene is constitutively expressed throughout development and mRNA is most likely maternally inherited. Lastly, three Minute alleles from the same locus were sequenced and two alleles found to contain a 22- bp deletion in exon 2, resulting in a truncated S3 protein, although wildtype levels of S3 mRNA and protein were detected in the viable heterozygous Minute alleles, possibly reflecting dosage compensation.
ACCESSION #
5322824

 

Related Articles

  • Yeast Ribosomal Protein S3 Has an Endonuclease Activity on APDNA. Sang-Oun Jung; Jae Yung Lee; Joon Kim // Molecules & Cells (Springer Science & Business Media B.V.);2001, Vol. 12 Issue 1, p84 

    The mammalian ribosomal protein S3 (rpS3) is a ponent of the 40S ribosomal subunit. It is known to function as a DNA repair enzyme, UV endonuclease III, which cleaves DNA that is irradiated by UV. It also has an endonuclease activity on AP DNA. In this report, the yeast ribosomal protein S3...

  • Interactions of human ribosomal protein S3 with intact and damaged DNA. Balueva, K. E.; Malygin, A. A.; Karpova, G. G.; Nevinsky, G. A.; Zharkov, D. O. // Molecular Biology;Mar2008, Vol. 42 Issue 2, p277 

    Human S3 (hS3) is a structural component of the ribosome and, in addition to its role in translation, possesses apurinic/apyrimidinic (AP) lyase activity, characteristic of DNA repair enzymes. Recombinant hS3 was isolated from inclusion bodies, refolded under different conditions, and tested for...

  • A Fluorophore-labeled Peptide of Human Ribosomal Protein S3 for the Detection of the 8-Oxoguanine within the Cells. Han, Se Hee; Hahm, Soo-Hyun; Tran, An Hue Vy; Park, Jin Woo; Chung, Ji Hyung; Park, Geon Tae; Han, Ye Sun // Bulletin of the Korean Chemical Society;Oct2015, Vol. 36 Issue 10, p2451 

    Detection and quantification of 8-oxo-7,8-dihydroguanine (8- oxoG) within cells are important for the study of the molecular mechanisms in cancer. Human ribosomal protein S3 ( hRpS3), which involved in DNA repair, has high binding affinity to 8- oxoG. We developed an imaging probe to detect 8-...

  • Translational regulation of RPA2 via internal ribosomal entry site and by eIF3a. Yin, Ji-Ye; Dong, Zi-Zheng; Liu, Ran-Yi; Chen, Juan; Liu, Zhao-Qian; Zhang, Jian-Ting // Carcinogenesis;Jun2013, Vol. 34 Issue 6, p1224 

    RPA2 is a subunit of a trimeric replication protein A (RPA) complex important for DNA repair and replication. Although it is known that RPA activity is regulated by post-translational modification, whether RPA expression is regulated and the mechanism therein is currently unknown. eIF3a, the...

  • K63 polyubiquitination is a new modulator of the oxidative stress response. Silva, Gustavo M; Finley, Daniel; Vogel, Christine // Nature Structural & Molecular Biology;Feb2015, Vol. 22 Issue 2, p116 

    Ubiquitination is a post-translational modification that signals multiple processes, including protein degradation, trafficking and DNA repair. Polyubiquitin accumulates globally during the oxidative stress response, and this has been mainly attributed to increased ubiquitin conjugation and...

  • Catalytic and Non-Catalytic Roles for the Mono-ADPRibosyltransferase Arr in the Mycobacterial DNA Damage Response. Stallings, Christina L.; Linda Chu; Li, Lucy X.; Glickman, Michael S. // PLoS ONE;2011, Vol. 6 Issue 7, p1 

    Recent evidence indicates that the mycobacterial response to DNA double strand breaks (DSBs) differs substantially from previously characterized bacteria. These differences include the use of three DSB repair pathways (HR, NHEJ, SSA), and the CarD pathway, which integrates DNA damage with...

  • Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis. Netz, Daili J. A.; Stümpfig, Martin; Doré, Carole; Mühlenhoff, Ulrich; Pierik, Antonio J.; Lill, Roland // Nature Chemical Biology;Oct2010, Vol. 6 Issue 10, p758 

    Cytosolic and nuclear iron-sulfur (Fe-S) proteins play key roles in processes such as ribosome maturation, transcription and DNA repair-replication. For biosynthesis of their Fe-S clusters, a dedicated cytosolic Fe-S protein assembly (CIA) machinery is required. Here, we identify the essential...

  • Diverse and dynamic functions of the Sir silencing complex. Guarente, L // Nature Genetics;Nov99, Vol. 23 Issue 3, p281 

    The yeast Sir protein complex has been implicated in transcriptional silencing and suppression of recombination. The Sir complex creates structured chromosomal domains at telomeres, silent mating-type loci and ribosomal DNA to invoke these functional states. Mechanistic insights into the...

  • Suppression of the poly(ADP-ribose) polymerase activity by DNA-dependent protein kinase in vitro. Ariumi, Yasuo; Masutani, Mitsuko; Copeland, Terry D; Mimori, Tuneyo; Sugimura, Takashi; Shimotohno, Kunitada; Ueda, Kunihiro; Hatanaka, Masakazu; Noda, Makoto // Oncogene;8/12/99, Vol. 18 Issue 32, p4616 

    It has been suggested that DNA-dependent protein kinase (DNA-PK) is a central component of DNA double-strand-break repair. The mechanism of DNA-PK action, however, has not been fully understood. Poly(ADP-ribose) polymerase (PARP) is another nuclear enzyme which has high affinity to DNA ends. In...

Share

Read the Article

Courtesy of VIRGINIA BEACH PUBLIC LIBRARY AND SYSTEM

Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics