• 제목/요약/키워드: CP1 domain

검색결과 39건 처리시간 0.024초

Structural characterization of the putative DNA-binding domain of CP2c and its relevance to zinc binding

  • Ryu, Ki-Sung;Jo, Ku-Sung;Kim, Na-Young;Jeon, Eun-Jae;Park, Sung Jean;Kim, Hyun-Hwi;Kim, Eun-Hee;Kim, Chan-Gil;Kim, Chul Geun;Won, Hyung-Sik
    • 한국자기공명학회논문지
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    • 제23권1호
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    • pp.20-25
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    • 2019
  • The transcription factor CP2c has been recently validated as an oncogenic protein that can serve as a promising target for anticancer therapy. We have recently documented that a recombinant protein corresponding to the putative DNA-binding region (residues 63-244) of CP2c adopted two different conformers, one of which is dominated by zinc binding. However, in the present study, a longer construct encompassing residues 63-302 appeared to form a single structural domain. This domain could be considered to adopt a functionally relevant fold, as the known specific binding of a dodecapeptide to this protein was evident. Hence, the residues 63-302 region rather than 63-244 can be regarded as a natively folded structural domain of CP2c. In addition, it was confirmed that zinc ions can bind to this putative DNA-binding domain of CP2c, which resulted in reduced stability of the protein. In this context, it is suggested that the mode of action of CP2c would resemble that of tumor suppressor p53.

Structural assessment of the tetramerization domain and DNA-binding domain of CP2c

  • Jo, Ku-Sung;Ryu, Ki-Sung;Yu, Hee-Wan;Lee, Seu-Na;Kim, Ji-Hun;Kim, Eun-Hee;Wang, Chae-Yeon;Kim, Chan-Gil;Kim, Chul Geun;Won, Hyung-Sik
    • 한국자기공명학회논문지
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    • 제22권4호
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    • pp.119-124
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    • 2018
  • Although the transcription factor CP2c has been recently validated as a promising target for development of novel anticancer therapy, its structure has not been solved yet. In the present study, the purified recombinant protein corresponding to the tetramerization domain of CP2c appeared to be well folded, whereas the Elf-1 domain showed a largely unfolded conformation. Particularly, the Elf-1 domain, which contains the putative DNA-binding region, showed a conformational equilibrium between relatively less-ordered and well-ordered conformers. Interestingly, addition of zinc shifted the equilibrium to the relatively more structured conformer, whereas zinc binding decreased the overall stability of the protein, leading to a promoted precipitation. Likewise, a dodecapeptide that has been suggested to bind to the Elf-1 domain also appeared to shift the conformational equilibrium and to destabilize the protein. These results constitute the first structural characterization of the CP2c domains and newly suggest that zinc ion might be involved in the conformational regulation of the protein.

The coat protein of Turnip crinkle virus is required a full-length to maintain suppressing activity to RNA silencing but no relation with eliciting resistance by N-terminal region in Arabidopsis.

  • Park, Chang-Won;Feng Qu;Tao Ren;T. Jack Morris
    • 한국식물병리학회:학술대회논문집
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    • 한국식물병리학회 2003년도 정기총회 및 추계학술발표회
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    • pp.76.1-76
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    • 2003
  • The coat protein (CP) of Turnip crinkle virus (TCV) is organized into 3 distinct domains, R domain (RNA-binding) connected by an arm, 5 domain and P domain. We have previously shown that the CP of TCV strongly suppresses RNA silencing, and have mapped N-terminal R domain of which is also the elicitor of resistance response in the Arabidopsis ecotype Di-17 carrying the HRT resistance gene. In order to map the region in the TCV CP that is responsible for silencing suppression, a series of CP mutants were constructed, transformed into Agrobacterium, coinfiltrated either with HC-Pro (the helper component proteinase of tobacco etch potyvirus) known as a suppressor of PTGS or GFP constructs into leaves of Nicotiana benthmiana expressing GFP transgenically. In the presence of HC-Pro, all CP mutants were well protected, accumulating mutant CP mRNAs and their proteins even 5 days post-infiltration (DPI). In the presence of GFP, some mutant constructs which showed the accumulation of CP mutants and GFP mRNAs at early stage but eventually degraded at 5 DPI. Only a mutant which carrying 4 amino acid deletion of R domain was tolerable to maintain suppressing activity, suggesting that the suppressing activity is not directly related with the eliciting activity. A transient assay also revealed that the mutants synthesized their proteins, suggesting that a full length of CP sequences and its intact structure are required to stabilize CP, which suppresses the RNA silencing.

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관측 행렬 산출 기법 별 DGNSS-CP 성능 비교 (DGNSS-CP Performance Comparison of Each Observation Matrix Calculation Method)

  • 신동현;임철순;석효정;윤동환;박병운
    • 한국항행학회논문지
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    • 제20권5호
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    • pp.433-439
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    • 2016
  • 저가형 GNSS (global navigation satellite system) 수신 모듈에 DGNSS (differential GNSS) 서비스를 적용하기 위한 방안으로 거리 영역의 보정정보를 위치 영역으로 투영한 후, stand-alone으로 산출한 위치에 적용하는 DGNSS-CP 방식이 제안된 바 있다. DGNSS-CP 를 상용 수신기 또는 휴대폰에 적용하기 위해서는 항법 방정식의 관측행렬을 이용하여 위치영역 투영 방정식을 구성하므로, 각 위성의 시선벡터를 산출하여야 한다. GNSS 항법 메시지, 배치 정보 등이 시선벡터 산출을 위하여 사용되는데, 각 방법에 따라 정확도와 연산량 등의 성능에 차이가 발생한다. 본 연구에서는 제시된 두 가지 시선벡터 산출 방식에 따라 DGNSS-CP의 성능에 어떠한 영향을 끼치는지 확인하기 위하여, Septentrio PolaRx4 Pro 수신기에서 stand-alone mode 로 저장된 데이터에 해당 알고리즘을 적용하였고, 배치 정보를 사용하는 방법이 궤도정보를 사용하는 방법에 비해 정확도 면에서는 그 성능이 RMS (root mean square) 0.1 m 가량 저하되는 반면, 연산량은 약 1/15수준으로 줄일 수 있음을 확인하였다.

Three Common Subunits in the Editing Domains of Class Ia tRNA Synthetases.

  • Lee, Keun-Woo;Kwon, Yong-Jung;Briggs, James M.
    • 산업기술연구
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    • 제24권B호
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    • pp.139-142
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    • 2004
  • To identify conserved structural or functional subunit(s) in the CP1 (editing) domains of class Ia tRNA synthetases, five available structures were compared and analyzed. Through sequence alignments of the CP1 domains, three conserved regions were found near the amino acid binding site in the editing domain. Structural overlapping of the three subunits clearly showed that there exist three common structural subunits in all of the five editing RS structures. The new alignment suggests a translocation movement of the CP1 domain caused by the binding with tRNA. Based on the experimental and modeling results, it is proposed that subunits 1 and 3 accommodate the incoming amino acid binding, while subunit 2 contributes to the interactions with the adenosine ring of the A76 to stabilize the overall tRNA binding.. Since these subunits are critical for the editing reaction, we expect that these key structures should be conserved through all class Ia editing RSs.

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Intrinsically disordered fold of a PIAS1-binding domain of CP2b

  • Jo, Ku-Sung;Jo, Hae-Ri;Kim, Chul Geun;Kim, Chan-Gil;Won, Hyung-Sik
    • 한국자기공명학회논문지
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    • 제18권1호
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    • pp.30-35
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    • 2014
  • The transcription factor CP2 regulates various biological systems at diverse tissues and cells. However, none of the four CP2 isoforms has been solved in structure yet. In particular, two different regions of the CP2b isoform have been characterized to interact with the PIAS1 in nucleus to regulate the ${\alpha}$-globin gene expression. Among them, in this study, the region encompassing residues 251-309 of CP2b was prepared as a recombinant protein and its solution structure was characterized by NMR spectroscopy. The results indicated that the CP2b(251-309) fold belongs to typical IDRs (intrinsically disordered regions), likely to facilitate promiscuous interactions with various target proteins. Unfortunately, however, its interaction with the N-terminal domain of PIAS1 (residues 1-70), which has been identified as one of the CP2b-binding sites, was not observed in the NMR-based titration experiments. Therefore, it could be postulated that the 251-309 region of CP2b would not contact with the PIAS1(1-70), but alternatively interact with another CP2b-binding region that encompasses residues 400-651 of PIAS1.

A Feasibility Test on the DGPS by Correction Projection Using MSAS Correction

  • Yoon, Dong Hwan;Park, Byungwoon;Yun, Ho;Kee, Changdon
    • Journal of Positioning, Navigation, and Timing
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    • 제3권1호
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    • pp.25-30
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    • 2014
  • Differential Global Positioning System-Correction Projection (DGPS-CP) algorithm, which has been suggested as a method of correcting pre-calculated position error by projecting range-domain correction to positional domain, is a method to improve the accuracy performance of a low price GPS receiver to 1 to 3 m, which is equivalent to that of DGPS, just by using a software program without changing the hardware. However, when DGPS-CP algorithm is actually realized, the error is not completely eliminated in a case where a reference station does not provide correction of some satellites among the visible satellites used in user positioning. In this study, the problem of decreased performance due to the difference in visible satellites between a user and a reference station was solved by applying the Multifunctional Transport Satellites (MTSAT) based Augmentation System (MASA) correction to DGPS-CP, instead of local DGPS correction, by using the Satellite Based Augmentation System (SBAS) operated in Japan. The experimental results showed that the accuracy was improved by 25 cm in the horizontal root mean square (RMS) and by 20 cm in the vertical RMS in comparison to that of the conventional DGPS-CP.

Three Common Subunits in Editing Domains of Class Ia tRNA Synthetases

  • Lee, Keun-Woo;Kwon, Yong-Jung;Briggs, James M.
    • Bulletin of the Korean Chemical Society
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    • 제28권2호
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    • pp.207-210
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    • 2007
  • To identify structural or functional common subunit(s) in the CP1 (editing) domains of class Ia tRNA synthetases, five available structures were compared and analyzed. Through the sequence alignments and structural overlapping of the CP1 domains, three conserved regions were identified near the amino acid binding site in the editing domain. Structural overlapping of the three subunits clearly showed the existence of three common structural subunits in all of the five editing RS structures. Based on the established experimental results and our modeling results, it is proposed that subunits 1 and 3 accommodate the incoming amino acid binding, while subunit 2 contributes to the interactions with the adenosine ring of the A76 to stabilize the overall tRNA binding. Since these subunits are critical for the editing reaction, we expect that these key structures should be conserved through the most class Ia editing RSs.

국내 재배마늘의 Cytochrome P450 유전자의 염기다형성 분포 (Nucleotide Polymorphisms of Cytochrome P450 Genes in Domestic Garlic Cultivars)

  • 권순태;정진보
    • 한국자원식물학회지
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    • 제31권5호
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    • pp.531-537
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    • 2018
  • 국내 재배종 마늘을 대상으로 상처(wound) 처리에 특이적으로 발현되는 Cyt. P450 cDNA (ORF 1,419 bp) 중 1,210~1,240 bp 사이에 존재하는 heme-binding domain (HB-domain)의 염기서열 다형성을 바탕으로 국내산 재배마늘의 HB-domain의 다형성 분포를 조사하였다. 국내 재배마늘에서 7개의 각각 다른 염기서열을 가진 HB-domain 마커를 탐색하였고, 전국 6개 지역의 재배농가에서 임의로 수집한 120개 마늘의 마커 종류별 분포도를 조사하였다. 경북, 충남, 충북, 강원지역에서 재배되는 한지형 마늘은 아미노산서열 FGGGRRICPG, DNA서열 5'-TTT/GGC/GGT/GGA/CGG/AGA/ATA/TGT/CCT/GGA-3'인 KP2형의 HB-domain을 가진 재배종이 51.3%로 가장 많이 분포하였고, KP1형 13.7%, CP형 11.3%, CM형 8.8%, KW2형 5% 및 기타 1.3%인 것으로 나타났다. 경남지역 재배지에서 수집한 난지형 마늘은 아미노산서열 FGAGRRICPG, DNA서열 '5-TTT/GGC/GCA/GGA/CGG/AGA/ATT/TGT/CCT/GGA-3'인 KM형이 52.5%로 가장 많았고, KP2형 22.5%, KW2형 5%, KP1 및 CP형이 각각 2.5%가 분포하는 것으로 나타났으나 CM형은 존재하지 않았다. 이 결과는 우리나라에 재배되는 마늘은 유전적으로 상당히 혼재된 상태로 존재하며, 특정 지역을 대표하는 유전적 특징을 가진 재배종을 단정하기는 어려운 것으로 판단된다.