• Title/Summary/Keyword: F-box

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The Ubiquitin-Proteasome System and F-box Proteins in Pathogenic Fungi

  • Liu, Tong-Bao;Xue, Chaoyang
    • Mycobiology
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    • v.39 no.4
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    • pp.243-248
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    • 2011
  • The ubiquitin-proteasome system is one of the major protein turnover mechanisms that plays important roles in the regulation of a variety of cellular functions. It is composed of E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 ubiquitin ligases that transfer ubiquitin to the substrates that are subjected to degradation in the 26S proteasome. The Skp1, Cullin, F-box protein (SCF) E3 ligases are the largest E3 gene family, in which the F-box protein is the key component to determine substrate specificity. Although the SCF E3 ligase and its F-box proteins have been extensively studied in the model yeast Saccharomyces cerevisiae, only limited studies have been reported on the role of F-box proteins in other fungi. Recently, a number of studies revealed that F-box proteins are required for fungal pathogenicity. In this communication, we review the current understanding of F-box proteins in pathogenic fungi.

Genome-wide survey and expression analysis of F-box genes in wheat

  • Kim, Dae Yeon;Hong, Min Jeong;Seo, Yong Weon
    • Proceedings of the Korean Society of Crop Science Conference
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    • 2017.06a
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    • pp.141-141
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    • 2017
  • The ubiquitin-proteasome pathway is the major regulatory mechanism in a number of cellular processes for selective degradation of proteins and involves three steps: (1) ATP dependent activation of ubiquitin by E1 enzyme, (2) transfer of activated ubiquitin to E2 and (3) transfer of ubiquitin to the protein to be degraded by E3 complex. F-box proteins are subunit of SCF complex and involved in specificity for a target substrate to be degraded. F-box proteins regulate many important biological processes such as embryogenesis, floral development, plant growth and development, biotic and abiotic stress, hormonal responses and senescence. However, little is known about the F-box genes in wheat. The draft genome sequence of wheat (IWGSC Reference Sequence v1.0 assembly) used to analysis a genome-wide survey of the F-box gene family in wheat. The Hidden Markov Model (HMM) profiles of F-box (PF00646), F-box-like (PF12937), F-box-like 2 (PF13013), FBA (PF04300), FBA_1 (PF07734), FBA_2 (PF07735), FBA_3 (PF08268) and FBD (PF08387) domains were downloaded from Pfam database were searched against IWGSC Reference Sequence v1.0 assembly. RNA-seq paired-end libraries from different stages of wheat, such as stages of seedling, tillering, booting, day after flowering (DAF) 1, DAF 10, DAF 20, and DAF 30 were conducted and sequenced by Illumina HiSeq2000 for expression analysis of F-box protein genes. Basic analysis including Hisat, HTseq, DEseq, gene ontology analysis and KEGG mapping were conducted for differentially expressed gene analysis and their annotation mappings of DEGs from various stages. About 950 F-box domain proteins identified by Pfam were mapped to wheat reference genome sequence by blastX (e-value < 0.05). Among them, more than 140 putative F-box protein genes were selected by fold changes cut-offs of > 2, significance p-value < 0.01, and FDR<0.01. Expression profiling of selected F-box protein genes were shown by heatmap analysis, and average linkage and squared Euclidean distance of putative 144 F-box protein genes by expression patterns were calculated for clustering analysis. This work may provide valuable and basic information for further investigation of protein degradation mechanism by ubiquitin proteasome system using F-box proteins during wheat development stages.

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Structure and Dynamics of Perfluoroalkanes and Their ${\beta}$-Cyclodextrin Inclusion Compounds Investigated by Solid-state $^{19}F$ MAS NMR

  • Tatsuno, Hiroto;Ando, Shinji
    • Proceedings of the Polymer Society of Korea Conference
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    • 2006.10a
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    • pp.305-305
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    • 2006
  • The molecular structure and dynamics of inclusion compounds (ICs) consisting of n-perfluoroalkane (PFA) guests and ${\Box}-cyclodextrin$ (${\Box}-CD$) host were investigated using $^{19}F$ magic angle spinning (MAS) and $^{1}H{\to}^{19}F$ cross polarization (CP) / MAS NMR spectroscopy with the aid of thermal analyses, FT-IR spectroscopy, X-ray diffraction, and $^{1}H{\to}^{19}F$ CP/MAS technique revealed that $C_{9}F_{20}$ molecules included in ${\Box}-CD$ undergo vigorous molecular motion and partly come out of the ${\Box}-CD$ channel above $80^{\circ}C$. In case of $C_{20}F_{42}/{\Box}-CD$, an exothermic peak is observed by differential scanning calorimetry (DSC) at ca. $40^{\circ}C$ which suggests that ${\Box}-CD$ molecules become mobile and commence rearrangements that form more ordered structures at higher temperatures.

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Members of Ectocarpus siliculosus F-box Family Are Subjected to Differential Selective Forces

  • Mahmood, Niaz;Moosa, Mahdi Muhammad;Matin, S. Abdul;Khan, Haseena
    • Interdisciplinary Bio Central
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    • v.4 no.1
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    • pp.1.1-1.7
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    • 2012
  • Background: The F-box proteins represent one of the largest families of proteins in eukaryotes. Apart from being a component of the ubiquitin (Ub)/26 S proteasome pathways, their regulatory roles in other cellular and developmental pathways have also been reported. One interesting feature of the genes encoding the proteins of this particular family is their variable selection patterns across different lineages. This resulted in the presence of lineage specific F-box proteins across different species. Findings: In this study, 48 non-redundant F-box proteins in E. siliculosus have been identified by a homology based approach and classified into three classes based on their variable C-terminal domains. A greater number of the F-box proteins have domains similar to the ones identified in other species. On the other hand, when the proteins having unknown or no C-terminal domain (as predicted by InterProScan) were analyzed, it was found that some of them have the polyglutamine repeats. To gain evolutionary insights on the genes encoding the F-box proteins, their selection patterns were analyzed and a strong positive selection was observed which indicated the adaptation potential of the members of this family. Moreover, four lineage specific F-box genes were found in E. siliculosus with no identified homolog in any other species. Conclusions: This study describes a genome wide in silico analysis of the F-box proteins in E. siliculosus which sheds light on their evolutionary patterns. The results presented in this study provide a strong foundation to select candidate sequences for future functional analysis.

The Smoothing of Rainfall Intensity - Duration - frequency Relationships curve by the Box-Cox Transformation (Box-Cox 변환에 의한 I-D-F 곡선의 평활화)

  • Lee, Hee-Chan;Seong, Kee-Won
    • Journal of Korea Water Resources Association
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    • v.36 no.2
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    • pp.153-159
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    • 2003
  • When available rainfall data is not sufficient, a rough tendency of I-D-F relationship appeared frequently. In fact, rainfall intensity on the curve shows abnormally higher value the longer rainfall duration is applied that gives rise to great confusion to apply a rainfall I-D-F relationships curve to a practical work, however, the research work will present a way to solve above mentioned problem by the use of the Box-Cox transformation formula for a given rainfall data. The study came to a conclusion that the Box-Cox transformation formula is satisfied to utilize in a practical work on the ground of analysis for rainfall data of Sancheong and Yeongcheon.

An analysis on the S-boxes of block ciphers in 3GPP (3GPP 블록 암호의 S-box 안전성 분석)

  • 장구영;강주성;이옥연;정교일
    • Journal of the Korea Institute of Information Security & Cryptology
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    • v.11 no.4
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    • pp.67-75
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    • 2001
  • 3GPP proposed f8 and f9 algorithms based on the block cipher KASUMI to provide the data confidentiality and integrity over a radio access link for IMT-2000(W-CDMA). Also 3GPP proposed Milenage algorithm based on the block cipher Rijndael to provide an example set for 3GPP authentication and key generation functions. In order to analyze the security of 3GPP algorithms, we must go ahead an analysis of security of KASUMI and Rijndael. Since S-box is an important point of security of block cipher, in this paper we analyze the S-boxes of KASUMI and Rijndael and compare the S-boxes of KASUMI with the S-box of Rijndael. Although KASUMI S9-box is bad for AC and SAC, we find that AC of KASUMI FI function containing S7-box and S9-box is equal to AC of Rijndael S-box and SAC of KASUMI FI function is better than SAC of Rijndael S-box.

Characterization of a Putative F-box Motif in Ibd1p/Bfalp, a Spindle Checkpoint Regulator of Budding Yeast Saccharomyces cerevisiae

  • Lee, Kyum-Jung;Hyung-Seo;Kiwon Song
    • Journal of Microbiology
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    • v.39 no.4
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    • pp.286-292
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    • 2001
  • During mitosis. the proper segregation of duplicated chromosomes is corrdinated by a spindle check-point. The bifurcated spindle checkpoint blocks cell cycle progression at metaphase by monitoring unattached kinetochores and inhibits mitotic exit in response to the misorientation of the mitotic spin- dle Ibd1p/Bfa1p is a spindle checkpoint regulator of budding yeast in the Bub2p checkpoint pathway for mitotic exit and its disruption abolishes mitotic arrest when proper organization of the mitotic spin-dls inhibited. Ibd1p/Bfa1p localizes to the spindle pole body, a microtublue-organizing center in yeast, and its overexpression arrests the cell cycle in 80% of cells with an enlarged budy at mitosis and in 20 % of cells with multiple buds. In this study, we found that the C-terminus of Ibd1p/Bfa1p phys-ically interacts with Skp1p, a key component of SCF (Skp1/cullin/F-box) complex for ubiquition-medi-ated proteolysis of cel cycle regulatores as well as an evolutionally conserved kinetochore protein for cell cycle progression. A putative F-box motif was found in the C-terminus of Ibd1p/Bfa1p and its function was investigated by making mutants of conserved residues in the motif. These Ibd1p/Bfa1p mutants of a putative F-box interacted with SKp1p in vitro by two-hybrid assays as wild type Ibd1p/Bfa1p. Also these Ibd1p/Bfa1p utants displayed the overexpression phenotypes of wild type Ibd1p, when over-expressed under inducible promoters . These results suggest that a putative F-box motif of Ibd1p/Bfa1p is not essential for the interaction with SKp1p and its function in mitotic exit and cytokinesis.

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A novel F-box protein with leucine-rich repeats affects defecation frequency and daumone response in Caenorhabditis elegans

  • Kim, Sung-Moon;Jang, Sang-Ho;Son, Na-Rae;Han, Ching-Tack;Min, Kwan-Sik;Lee, Hak-Kyo;Hwang, Sue-Yun
    • Animal cells and systems
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    • v.16 no.4
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    • pp.280-288
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    • 2012
  • Targeted degradation of proteins through ubiquitin-mediated proteolysis is an important control mechanism in various cellular processes. The process of ubiquitin conjugation is achieved by three enzyme complexes, among which the ubiquitin ligase complex (E3) is in charge of substrate specificity. The SCF (SKP1-CUL1-F-box) family portrays the largest and the most characterized member of the E3 ligases. For each SCF complex, the ubiquitination target is recognized by the F-box protein subunit, which interacts with the substrate through a unique C-terminal domain. We have characterized a novel F-box protein CFL-1 that represents a single LRR-type F-box (FBXL) in the Caenorhabditis elegans genome. CFL-1 is highly homologous to FBXL20 and FBXL2 of mammals, which are known to regulate synaptic vesicle release and cell cycle, respectively. A green fluorescence protein (GFP)-reporter gene fused to the cfl-1 promoter showed restricted expression around the amphid and the anus. Modulation of CFL-1 activity by RNAi affected the time interval between defecations. RNAi-treated worms also exhibited reduced tendency to form dauer when exposed to daumone. The potential involvement of CFL-1 in the control of defecation and pheromone response adds to the ever expanding list of cellular processes controlled by ubiquitin-mediated proteolysis in C. elegans. We suggest that CFL-1, as a single LRR-type F-box protein in C. elegans, may portray a prototype gene exerting diverse functions that are allocated among multiple FBXLs in higher organisms.

Modification of Finite Field Based S-box and Its Transform Domain Analysis (유한체 연산 기반의 치환상자 설계 및 변환 영역 특성 분석)

  • Jin, Seok-Yong;Baek, Jong-Min;Song, Hong-Yeop
    • Journal of the Korea Institute of Information Security & Cryptology
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    • v.17 no.3
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    • pp.3-15
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    • 2007
  • In this paper, we propose a simple scheme which produces a new S-box from a given S-box. We use well-known conversion technique between the polynomial functions over a finite field $F_{2^n}$ and the boolean functions from $F_2^n$ to $F_2$. We have applied this scheme to Rijndael S-box and obtained 29 new S-boxes, whose linear complexities are improved. We investigate their cryptographic properties via transform domain analysis.

Effect of E-box and E2F Binding Site on Transcriptional Activity in MCM Promoter (MCM promoter에서 E-box와 E2F 결합부위가 전사활성에 미치는 영향)

  • 권현주
    • Journal of Life Science
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    • v.14 no.5
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    • pp.732-740
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    • 2004
  • MCM proteins are essential for eukaryotic DNA replication, playing roles in the initiation and elongation of DNA replication. MCM proteins expression is much higher in malignant tissues than normal tissues. Several reports have indicated the usefulness of MCM proteins as markers of cancer cells in histopathological diagnosis. However, the cause of enhanced expression of MCM proteins in cancer cells remain to be clarified. The purpose of this study is to examine the relative transcriptional activities of human mcm gene promoters in cancer and normal cells. The minimal promoter region required for transcription of a luciferase reporter gene was contained an E-box and one E2F site. In addition, luciferase activities from mcm7 and mcm2 promoter/luciferase gene reporter constructs were significantly increased in cancer cells at 8 times compared with normal cells. E-box and E2F binding site in the promoter of mcm genes are responsible for different mechanism of transcription regulation on the cellular environment.