http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Backbone assignment of the anticodon binding domain of human Glycyl-tRNA synthetase
Mushtaq, Ameeq Ul,Cho, Hye Young,Byun, Youngjoo,Jeon, Young Ho Korean Magnetic Resonance Society 2016 Journal of the Korean Magnetic Resonance Society Vol.20 No.2
Backbone $^1H$, $^{13}C$ and $^{15}N$ resonance assignments are presented for the anticodon binding domain (residues 557-674) of human glycyl-tRNA synthetase (GRS). Role of the anticodon binding domain (ABD) of GRS as an anticancer ligand has recently been reported and its role in other diseases like Charcot-Marie-Tooth (CMT) and polymyositis have increased its interest. NMR assignments were completed using the isotope [$^{13}C/^{15}N$]-enriched protein and chemical shifts based secondary structure analysis with TALOS+ demonstrate similar secondary structure as reported in X-ray structure PDB 2ZT8, except some C-terminal residues. NMR signals from the N-terminal residues 557 to 571 and 590 to 614 showed very weak or no signals exhibiting dynamics or conformational exchange in NMR timescale.
Backbone assignment of the anticodon binding domain of human Glycyl-tRNA synthetase
Ameeq Ul Mushtaq,조혜영,변영주,전영호 한국자기공명학회 2016 Journal of the Korean Magnetic Resonance Society Vol.20 No.2
Backbone 1H, 13C and 15N resonance assignments are presented for the anticodon binding domain (residues 557-674) of human glycyl-tRNA synthetase (GRS). Role of the anticodon binding domain (ABD) of GRS as an anticancer ligand has recently been reported and its role in other diseases like Charcot–Marie–Tooth (CMT) and polymyositis have increased its interest. NMR assignments were completed using the isotope [13C/15N]-enriched protein and chemical shifts based secondary structure analysis with TALOS+ demonstrate similar secondary structure as reported in X-ray structure PDB 2ZT8, except some C-terminal residues. NMR signals from the N-terminal residues 557 to 571 and 590 to 614 showed very weak or no signals exhibiting dynamics or conformational exchange in NMR timescale.
Ligand-Mediated Folding of the OmpA Periplasmic Domain from <i>Acinetobacter baumannii</i>
Mushtaq, Ameeq Ul,Park, Jeong Soon,Bae, Sung-Hun,Kim, Hye-Yeon,Yeo, Kwon Joo,Hwang, Eunha,Lee, Ki Yong,Jee, Jun-Goo,Cheong, Hae-Kap,Jeon, Young Ho Published for the Biophysical Society by the Rocke 2017 Biophysical journal Vol.112 No.10
<P>The periplasmic domain of OmpA from Acinetobacter baumannii (AbOmpA-PD) binds to diaminopimelate and anchors the outer membrane to the peptidoglycan layer in the cell wall. Although the crystal structure of AbOmpA-PD with its ligands has been reported, the mechanism of ligand-mediated folding of AbOmpA remains elusive. Here, we report that in vitro refolded apo-AbOmpA-PD in the absence of ligand exists as a mixture of two partially folded forms in solution: mostly unfolded (apo-state I) and hololike (apo-state II) states. Binding of the diaminopimelate or glycine ligand induced complete folding of AbOmpA-PD. The apo-state I was highly flexible and contained some secondary structural elements, whereas the apo-state II closely resembled the holo-state in terms of both structure and backbone dynamics, except for the ligand-binding region. N-15-relaxation-dispersion analyses for apo-state II revealed substantial motion on a millisecond timescale of residues in the H3 helix near the ligand-binding site, with this motion disappearing upon ligand binding. These results provide an insight into the ligand-mediated folding mechanism of AbOmpA-PD in solution.</P>
Mushtaq, Ameeq Ul,Lee, Yejin,Hwang, Eunha,Bang, Jeong Kyu,Hong, Eunmi,Byun, Youngjoo,Song, Ji-Joon,Jeon, Young Ho Academic Press 2018 Biochemical and biophysical research communication Vol. No.
<P><B>Abstract</B></P> <P>MeCP2 is a chromatin associated protein which is highly expressed in brain and relevant with Rett syndrome (RTT). There are AT-hook motifs in MeCP2 which can bind with AT-rich DNA, suggesting a role in chromatin binding. Here, we report the identification and characterization of another AT-rich DNA binding motif (residues 295 to 313) from the C-terminal transcription repression domain of MeCP2 by nuclear magnetic resonance (NMR) and isothermal calorimetry (ITC). This motif shows a micromolar affinity to AT-rich DNA, and it binds to the minor groove of DNA like AT-hook motifs. Together with the previous studies, our results provide an insight into a critical role of this motif in chromatin structure and function.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Basic cluster region (residues 295 to 313) in the MeCP2 binds to AT-rich DNA. </LI> <LI> NMR relaxation data identified that IKKRKTRE is critical for binding. </LI> <LI> Basic cluster peptide binds to the minor groove of DNA, similar to AT-hooks. </LI> </UL> </P>
Purification and biophysical characterization of the AIMP2-DX2 protein
Jha, Roshan,Cho, Hye Young,Mushtaq, Ameeq Ul,Lee, Kiho,Kim, Dae Gyu,Kim, Sunghoon,Jeon, Young Ho Elsevier 2017 Protein expression and purification Vol.132 No.-
<P><B>Abstract</B></P> <P>Besides their primary role in protein synthesis, aminoacyl-tRNA synthetases (AARSs) are involved in several non-canonical processes such as apoptosis, inflammation and angiogenesis through their interactions with various cellular proteins. Nine of these AARSs interact with three aminoacyl-tRNA synthetase interacting multifunctional proteins (AIMPs), forming a multi-synthetase complex (MSC) in eukaryotes. Among the three AIMPs, AIMP2 is involved in controlling cell proliferation and apoptosis. However, a splicing variant of AIMP2 lacking exon 2, referred to as AIMP2-DX2, is oncogenic and compromises the pro-apoptotic activity of AIMP2 by competing with it for p53 and TRAF2. AIMP2-DX2 is also an inhibitor of p14arf activity. Thus, there is a pressing need for structural insight into the oncogenic role of AIMP2-DX2. In this study, we expressed and purified human AIMP2-DX2 using a SUMO tag to more than 95% purity and a yield of 10 mg/L. We have used size exclusion chromatography, glutaraldehyde cross-linking, dynamic light scattering and nuclear magnetic resonance spectroscopy to characterize its biophysical properties. These data indicate monomer-dimer equilibrium of AIMP2-DX2 in solution. These results form the basis for the structure-function study of oncogenic AIMP2-DX2.</P> <P><B>Highlights</B></P> <P> <UL> <LI> AIMP2-DX2 is oncogenic and compromises the pro-apoptotic activity of AIMP2. </LI> <LI> High purity with mg quantity of AIMP2-DX2 was successfully purified. </LI> <LI> AIMP2-DX2 exists in monomer-dimer equilibrium in solution. </LI> </UL> </P>
Chemical inhibition of prometastatic lysyl-tRNA synthetase–laminin receptor interaction
Kim, Dae Gyu,Lee, Jin Young,Kwon, Nam Hoon,Fang, Pengfei,Zhang, Qian,Wang, Jing,Young, Nicolas L,Guo, Min,Cho, Hye Young,Mushtaq, Ameeq Ul,Jeon, Young Ho,Choi, Jin Woo,Han, Jung Min,Kang, Ho Woong,Joo NATURE PUBLISHING GROUP 2014 NATURE CHEMICAL BIOLOGY Vol. No.
Lysyl-tRNA synthetase (KRS), a protein synthesis enzyme in the cytosol, relocates to the plasma membrane after a laminin signal and stabilizes a 67-kDa laminin receptor (67LR) that is implicated in cancer metastasis; however, its potential as an antimetastatic therapeutic target has not been explored. We found that the small compound BC-K-YH16899, which binds KRS, impinged on the interaction of KRS with 67LR and suppressed metastasis in three different mouse models. The compound inhibited the KRS-67LR interaction in two ways. First, it directly blocked the association between KRS and 67LR. Second, it suppressed the dynamic movement of the N-terminal extension of KRS and reduced membrane localization of KRS. However, it did not affect the catalytic activity of KRS. Our results suggest that specific modulation of a cancer-related KRS-67LR interaction may offer a way to control metastasis while avoiding the toxicities associated with inhibition of the normal functions of KRS.