Journal of Microbiology

Research Support, Non-U.S. Gov'ts

Novel nuclear targeting coiled-coil protein of Helicobacter pylori showing Ca2+-independent, Mg2+-dependent DNase I activity: Young Chul Kwon , Sinil Kim , Yong Seok Lee , Je Chul Lee , Myung-Je Cho , Woo-Kon Lee , Hyung-Lyun Kang , Jae-Young Song , Seung Chul Baik , Hyeon Su Ro; J. Microbiol. 2016;54(5):387-395. Published online April 20, 2016; DOI: https://doi.org/10.1007/s12275-016-5631-9

43 View
0 Download
5 Crossref

HP0059, an uncharacterized gene of Helicobacter pylori, encodes a 284-aa-long protein containing a nuclear localization sequence (NLS) and multiple leucine-rich heptad repeats. Effects of HP0059 proteins in human stomach cells were assessed by incubation of recombinant HP0059 proteins with the AGS human gastric carcinoma cell line. Wild-type HP0059 proteins showed cytotoxicity in AGS cells in a concentrationdependent manner, whereas NLS mutant protein showed no effect, suggesting that the cytotoxicity is attributed to host nuclear localization. AGS cells transfected with pEGFP-HP0059 plasmid showed strong GFP signal merged to the chromosomal DNA region. The chromosome was fragmented into multiple distinct dots merged with the GFP signal after 12 h of incubation. The chromosome fragmentation was further explored by incubation of AGS chromosomal DNA with recombinant HP0059 proteins, which leaded to complete degradation of the chromosomal DNA. HP0059 protein also degraded circular plasmid DNA without consensus, being an indication of DNase I activity. The DNase was activated by MgCl2, but not by CaCl2. The activity was completely blocked by EDTA. The optimal pH and temperature for DNase activity were 7.0–8.0 and 55°C, respectively. These results indicate that HP0059 possesses a novel DNase I activity along with a role in the genomic instability of human gastric cells, which may result in the transformation of gastric cells.

Citations

Citations to this article as recorded by

The Identification of a Novel Nucleomodulin MbovP467 of Mycoplasmopsis bovis and Its Potential Contribution in Pathogenesis
Abdul Raheem, Doukun Lu, Abdul Karim Khalid, Gang Zhao, Yingjie Fu, Yingyu Chen, Xi Chen, Changmin Hu, Jianguo Chen, Huanchun Chen, Aizhen Guo
Cells.2024; 13(7): 604. CrossRef
Molecular Coevolution of Nuclear and Nucleolar Localization Signals inside the Basic Domain of HIV-1 Tat
Margarita A. Kurnaeva, Arthur O. Zalevsky, Eugene A. Arifulin, Olga M. Lisitsyna, Anna V. Tvorogova, Maria Y. Shubina, Gleb P. Bourenkov, Maria A. Tikhomirova, Daria M. Potashnikova, Anastasia I. Kachalova, Yana R. Musinova, Andrey V. Golovin, Yegor S. Va
Journal of Virology.2022;[Epub] CrossRef
Bacterial nucleomodulins and cancer: An unresolved enigma
Abdul Arif Khan, Zakir Khan
Translational Oncology.2021; 14(1): 100922. CrossRef
TatD DNases of African trypanosomes confer resistance to host neutrophil extracellular traps
Kai Zhang, Ning Jiang, Hongyu Chen, Naiwen Zhang, Xiaoyu Sang, Ying Feng, Ran Chen, Qijun Chen
Science China Life Sciences.2021; 64(4): 621. CrossRef
Origin of the nuclear proteome on the basis of pre-existing nuclear localization signals in prokaryotic proteins
Olga M. Lisitsyna, Margarita A. Kurnaeva, Eugene A. Arifulin, Maria Y. Shubina, Yana R. Musinova, Andrey A. Mironov, Eugene V. Sheval
Biology Direct.2020;[Epub] CrossRef

Removal of Contaminating TEM-la β-Lactamase Gene from Removal of Contaminating TEM-la β-Lactamase Gene from: Jae Seok Song , Jung Hun Lee , Jung-Hyun Lee , Byeong Chul Jeong , Won-Keun Lee , Sang Hee Lee; J. Microbiol. 2006;44(1):126-128.; DOI: https://doi.org/2326 [pii]

29 View
0 Download

Abstract: This study confirms that Taq DNA polymerase could be contaminated with the blaTEM-1a gene. It also proposes two different methods that could be used to overcome DNA contamination: (i) DNase I treatment prior to PCR amplification; and (ii) the use of a highly purified Taq DNA polymerase which was devoid of detectable contamination.

Alteration of chromosomal structure within β-Tubulin and flagellar calmodulin genes during differentiation of Naegleria gruberi Amebae into Flagellates: Bok, Jin Woong , Lee, Joo Hun; J. Microbiol. 1995;33(3):222-227.

37 View
0 Download

Abstract: We have examined DNase I sensitivity of β-tubulin and flagellar calmodulin genes which are transiently and coordinately activated differentiation of Naegleria gruberi amebae into flagellates. The DNase I sensitivity of β-tubulin and flagellar calmodulin genes changed in parallel with the changes in transcriptional activity of the respective genes during differentiation. The two genes were resistant to DNase I inamebae stage when transcription of the two genes was inactive. Forty minutes after initiation of differentiation, when the two genes were most actively being transcribed, the two genes showed the highest sensitsivity to DNase I. One hundred and twenty minutes after initiation, the differentiation was completed and transcriptional activity of the two genes decreased to a low level. At this stage, the two genes were resistant to DNase I treatment like the ones at the ameba stage. This change in the DNase I sensitivity of the two genes was not observed when transcription of the two genes was blocked by adding cycloheximide at the beginning of differentiation.

Role of chromatin structure in HMRE mediated transcriptional repression of the HSP82 heat shock gene: Lee, See Woo , Gross, Davis S.; J. Microbiol. 1996;34(1):40-48.

35 View
0 Download

Abstract: We have examined the chromatin structure of the HMRE/HSP82 and HMRa/HSP82 allels using three complementary approaches : DNase I chromating footprinting, micrococcal nuclease (MNase) nucleosome-protected ladder assay, and an in vivo E. coli dam methylase accessibility assay. The footprinting results indicate that the promoter and silencer sequences are assembled into nucleoprotein complexes which exhibit no detectable change in structure, despite a 70-fold range in expression levels. In addition, the promoter region of the HMRa/HSP82 allele is cleaved randomly by MNase in all cases, indicating the absence of anonical nucleosomes over this region irrespective of SIR4 or heat-shock. Finally, no discernible difference in the accessibility of the HMRE/HSP82 locus to dam methylase in SIR4 vs. sir4 cells was seen, which again suggests that the chromatin structure of HMRE/HSP82 allele is identical regardless of SIR4. Altogether, our results indicate that in contrast to other observations of the silent mating-type loci, no discernible structural alteration is detected at either HMR/HSP82 allele regardless of SIR genetic background or transcriptional state of the gene.

Reorganization of chromatin conformation from an active to an inactive state after cessation of transcription: Lee , Myeong Sok; J. Microbiol. 1996;34(1):54-60.

32 View
0 Download

Abstract: Taking advantage of the heat inducible HSP82 gene in yeast, chromatin structure after transcription cessation was investigated. Alteration of chromating conformation within the HSP82 gene transcription unit into an active state has been shown to correlate with its transcriptional induction. It was thus of interest to examine whether the active chromatin state within the HSP82 mRNA analysis, the gene ceased its transcription within a few hours of cultivation at a normal condition after heat induction. In this condition, an active chromatin conformation in the HSP82 gene body was changed into an inactive state which was revealed by DNase I resistance and by typical nucleosomal cutting periodicity in the corresponding chromatin. These results thus ruled out the possibility of a long-term maintenance of the DNase I sensitive chromatin after transcription cessation. DNA replication may be a critical event for the chromatin reprogramming.

First
Prev
Page of 1
Next
Last

Search