• 제목/요약/키워드: domain sequence

검색결과 773건 처리시간 0.019초

Monoacylglycerol O-acyltransferase 1 (MGAT1) localizes to the ER and lipid droplets promoting triacylglycerol synthesis

  • Lee, Yoo Jeong;Kim, Jae-woo
    • BMB Reports
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    • 제50권7호
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    • pp.367-372
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    • 2017
  • Monoacylglycerol acyltransferase 1 (MGAT) is a microsomal enzyme that catalyzes the synthesis of diacylglycerol (DAG) and triacylglycerol (TAG). However, the subcellular localization and catalytic function domain of this enzyme is poorly understood. In this report, we identified that murine MGAT1 localizes to the endoplasmic reticulum (ER) under normal conditions, whereas MGAT1 co-localize to the lipid droplets (LD) under conditions of enriching fatty acids, contributing to TAG synthesis and LD expansion. For the enzyme activity, both the N-terminal transmembrane domain and catalytic HPHG motif are required. We also show that the transmembrane domain of MGAT1 consists of two hydrophobic regions in the N-terminus, and the consensus sequence FLXLXXXn, a putative neutral lipid-binding domain, exists in the first transmembrane domain. Finally, MGAT1 interacts with DGAT2, which serves to synergistically increase the TAG biosynthesis and LD expansion, leading to enhancement of lipid accumulation in the liver and fat.

Effective Biological Sequence Alignment Method using Divide Approach

  • 최해원;김상진;피수영
    • 한국산업정보학회논문지
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    • 제17권6호
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    • pp.41-50
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    • 2012
  • This paper presents a new sequence alignment method using the divide approach, which solves the problem by decomposing sequence alignment into several sub-alignments with respect to exact matching subsequences. Exact matching subsequences in the proposed method are bounded on the generalized suffix tree of two sequences, such as protein domain length more than 7 and less than 7. Experiment results show that protein sequence pairs chosen in PFAM database can be aligned using this method. In addition, this method reduces the time about 15% and space of the conventional dynamic programming approach. And the sequences were classified with 94% of accuracy.

DOMAIN OF EULER-TOTIENT MATRIX OPERATOR IN THE SPACE 𝓛p

  • Demiriz, Serkan;Erdem, Sezer
    • Korean Journal of Mathematics
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    • 제28권2호
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    • pp.361-378
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    • 2020
  • The most apparent aspect of the present study is to introduce a new sequence space 𝚽(𝓛p) derived by double Euler-Totient matrix operator. We examine its topological and algebraic properties and give an inclusion relation. In addition to those, the α-, β(bp)- and γ-duals of the space 𝚽(𝓛p) are determined and finally, some 4-dimensional matrix mapping classes related to this space are characterized.

On Some Spaces Isomorphic to the Space of Absolutely q-summable Double Sequences

  • Capan, Husamettin;Basar, Feyzi
    • Kyungpook Mathematical Journal
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    • 제58권2호
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    • pp.271-289
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    • 2018
  • Let 0 < q < ${\infty}$. In this study, we introduce the spaces ${\mathcal{BV}}_q$ and ${\mathcal{LS}}_q$ of q-bounded variation double sequences and q-summable double series as the domain of four-dimensional backward difference matrix ${\Delta}$ and summation matrix S in the space ${\mathcal{L}}_q$ of absolutely q-summable double sequences, respectively. Also, we determine their ${\alpha}$- and ${\beta}-duals$ and give the characterizations of some classes of four-dimensional matrix transformations in the case 0 < q ${\leq}$ 1.

NMR Study of Consensus DNA-binding Site for Arabidopsis thaliana Class I Transcription Factor AtTCP1

  • Choi, Yong-Geun;Kim, Hee-Eun;Lee, Joon-Hwa
    • 한국자기공명학회논문지
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    • 제17권2호
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    • pp.76-80
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    • 2013
  • The TCP domain is a DNA-binding domain present in plant transcription factors and has a similar structural feature to the bHTH motif of eukaryotic transcription factors. The imino proton exchange study has been performed for the DNA duplex containing the consensus DNA-binding site for the AtTCP11 transcription factor. The first two base pairs in the consensus 5'-GTGGG-3' sequence are relatively very unstable but lead to greater stabilization of the neighboring two G C base pairs. These unique dynamic features of the five base pairs in the consensus DNA sequence might play crucial roles in the effective DNA binding of the AtTCP11 protein.

기능 도메인 예측을 위한 유전자 서열 클러스터링 (Gene Sequences Clustering for the Prediction of Functional Domain)

  • 한상일;이성근;허보경;변윤섭;황규석
    • 제어로봇시스템학회논문지
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    • 제12권10호
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    • pp.1044-1049
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    • 2006
  • Multiple sequence alignment is a method to compare two or more DNA or protein sequences. Most of multiple sequence alignment tools rely on pairwise alignment and Smith-Waterman algorithm to generate an alignment hierarchy. Therefore, in the existing multiple alignment method as the number of sequences increases, the runtime increases exponentially. In order to remedy this problem, we adopted a parallel processing suffix tree algorithm that is able to search for common subsequences at one time without pairwise alignment. Also, the cross-matching subsequences triggering inexact-matching among the searched common subsequences might be produced. So, the cross-matching masking process was suggested in this paper. To identify the function of the clusters generated by suffix tree clustering, BLAST and CDD (Conserved Domain Database)search were combined with a clustering tool. Our clustering and annotating tool consists of constructing suffix tree, overlapping common subsequences, clustering gene sequences and annotating gene clusters by BLAST and CDD search. The system was successfully evaluated with 36 gene sequences in the pentose phosphate pathway, clustering 10 clusters, finding out representative common subsequences, and finally identifying functional domains by searching CDD database.

Localization of F plasmid SopB protein and Gene silencing via protein-mediated subcellular localization of DNA

  • Kim Sook-Kyung;James C. Wang
    • 한국미생물학회:학술대회논문집
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    • 한국미생물학회 2000년도 추계학술발표대회
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    • pp.15-23
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    • 2000
  • The subcellular localization of the SopB protein, which is encoded by the Escherichia coli F plasmid and is involved in the partition of the single-copy plasmid, was directly visualized through the expression of the protein fused to the jellyfish green fluorescent protein (GFP). The fusion protein was found to localize to positions close but not at the poles of exponentially growing cells. Examination of derivatives of the fusion protein lacking various regions of SopB suggests that the signal for the cellular localization of SopB resides in a region close to its N terminus. Overexpression of SopB led to silencing of genes linked to, but well-separated from, a cluster of SopB-binding sites termed sopC. In this SopB-mediated repression of sopC-linked genes, all but the N-terminal 82 amino acids of SopB can be replaced by the DNA-binding domain of a sequence-specific DNA -binding protein, provided that the sopC locus is also replaced by the recognition sequence of the DNA-binding domain. These results suggest a mechanism of gene silencing: patches of closely packed DNA-binding protein is localized to specific cellular sites; such a patch can capture a DNA carrying the recognition site of the DNA -binding domain and sequestrate genes adjacent to the recognition site through nonspecific binding of DNA.

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Cytosolic domain regulates the calcium sensitivity and surface expression of BEST1 channels in the HEK293 cells

  • Kwon Woo Kim;Junmo Hwang;Dong-Hyun Kim;Hyungju Park;Hyun-Ho Lim
    • BMB Reports
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    • 제56권3호
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    • pp.172-177
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    • 2023
  • BEST family is a class of Ca2+-activated Cl- channels evolutionary well conserved from bacteria to human. The human BEST paralogs (BEST1-BEST4) share significant amino acid sequence homology in the N-terminal region, which forms the transmembrane helicases and contains the direct calcium-binding site, Ca2+-clasp. But the cytosolic C-terminal region is less conserved in the paralogs. Interestingly, this domain-specific sequence conservation is also found in the BEST1 orthologs. However, the functional role of the C-terminal region in the BEST channels is still poorly understood. Thus, we aimed to understand the functional role of the C-terminal region in the human and mouse BEST1 channels by using electrophysiological recordings. We found that the calcium-dependent activation of BEST1 channels can be modulated by the C-terminal region. The C-terminal deletion hBEST1 reduced the Ca2+-dependent current activation and the hBEST1-mBEST1 chimera showed a significantly reduced calcium sensitivity to hBEST1 in the HEK293 cells. And the C-terminal domain could regulate cellular expression and plasma membrane targeting of BEST1 channels. Our results can provide a basis for understanding the C-terminal roles in the structure-function of BEST family proteins.

Sequence Homologies of GTP-binding Domains of Rab and Rho between Plants and Yeast/Animals Suggest Structural and Functional Similarities

  • Lee, Ji-Yeon;Lee, Dong-Hee
    • Journal of Plant Biology
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    • 제39권2호
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    • pp.85-92
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    • 1996
  • Small GTP-binding proteins are divided into three major group: Ras, Rho and Ypt/Rab. They have the conserved regions designed G1 to G5 that are critical in GDP/GTP exchange, GTP-induced conformational change and GTP hydrolysis. We isolated and characterized genomic DNA or cDNAfragments encoding G1 to G3 domains of small GTP-binding protein Rab and Rho from several plant species using two different PCR-based cloning strategies. Seven rab DNA fragments were isolated from 4 different plants, mung-bean, tobacco, rice and pepper using two degenerate primers corresponding to the GTP-binding domain G1 and G3 in small GTP-binding proteins. The amino acid sequences among these rab DNA fragments and other known small GTP-binding proteins shows that they belong to the Ypt/Rab family. Six rho DNA fragments were isolated from 5 different plants, mung-bean, rice, Arabidopsis, Allium and Gonyaulax using the nested PCR method that involves four degenerate primers corresponding to the GTP-binding domain G1, G3 and G4. The rho DNA fragments cloned show more than 90% homology to each other. Sequence comparison between plant and other known Rho family genes suggests that they are closely related (67 to 82% amino acid identity). Sequence analysis and southern blot analysis of rab and rho in mung-bean suggest than thses genes are encoded by multigene family in mung-bean.

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Molecular characterization of a lectin, BPL-4, from the marine green alga Bryopsis plumosa (Chlorophyta)

  • Han, Jong-Won;Yoon, Kang-Sup;Jung, Min-Gui;Chah, Kyong-Hwa;Kim, Gwang-Hoon
    • ALGAE
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    • 제27권1호
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    • pp.55-62
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    • 2012
  • A novel lectin specific to N-acetyl-D-galactosamine as well as N-acetyl-D-glucosamine was isolated from Bryopsis plumosa and named as BPL-4. Sodium dodecyl sulfate polyacrylamide gel electrophorese (SDS-PAGE) and matrix-assisted laser desorption / ionization-time of flight (MALDI-TOF) mass spectrometry data showed that this lectin was a monomeric protein with molecular weight 12.9 kDa. The N-terminal amino acid sequences of the lectin were determined by Edman degradation and the full cDNA sequence encoding this lectin was obtained using the degenerate primers designed from the amino acid sequence. The size of the cDNA was 414 bp containing single open reading frame (ORF) encoding the lectin precursor. The homology analysis showed that this lectin might belong to H lectin group. BPL-4 showed high sequence similarity (60.6%) to BPL-3, which is a previously reported lectin from the same species. The comparative analysis on the lectin's primary structure showed two conserved domains including one possible active domain of H lectin group.