• Title/Summary/Keyword: eIF1A

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Developmental Expression of Eukaryotic Initiation Factor 4E (eIF4E) and eIF4E-binding Protein 1 (eIF4EBP1) in Rat Hippocampal Neurons (발생단계별 해마신경세포에서 eIF4E 및 eIF4EBP1의 표현)

  • Park, Jaewan;Moon, Il Soo
    • Journal of Life Science
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    • v.23 no.7
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    • pp.941-946
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    • 2013
  • Local protein synthesis at subsynaptic sites plays a key role in the regulation of the protein composition in local domains. In this study, we carried out immunocytochemistry of cultured rat hippocampal neurons in various developmental stages to investigate the expression of eIF4E and its binding protein, eIF4EBP1. Both proteins were distributed in dendrites. In addition, eIF4EBP1 was highly expressed in the nucleus throughout the development, whereas eIF4E was not expressed in the nucleus. Punctate expression of eIF4E and eIF4EBP1 was evident in DIV 3. The colocalization rates of eIF4E or eIF4EBP1 puncta with PSD95 were higher in the dendrogenic than in the mature stages. In contrast, the colocalization rates of eIF4E and eIF4EBP1 puncta were higher in the mature than in the dendrogenic stages. As eIF4E is inactive when it is bound to eIF4EBP1, these data indicate that most dendritic eIF4E's are active during development but that they are mostly under inhibition in mature neurons.

Overexpression of Clast4 Reduces Cell Proliferation (Clast4의 과발현에 의한 세포 증식의 감소)

  • Kang, Minkook;Han, Seung Jin
    • Journal of Life Science
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    • v.24 no.10
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    • pp.1144-1150
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    • 2014
  • The eIF4E protein is the key regulator of translation initiation. The interaction of eIF4E with eIF4G triggers the translation of mRNA, and several proteins interrupt this association to modulate translation. Human 4E-T is one of the eIF4E-binding partners that represses the translation of bound mRNAs, and it is involved in the transport of eIF4E to processing bodies (P-bodies). Although Clast4, the mouse homolog of human 4E-T, might play critical roles in the regulation of translation, its properties are not well known. In this report, we deciphered the properties of Clast4 by determining its phosphorylation state, binding to eIF4E, and effects of overexpression on cell proliferation. Clast4 was phosphorylated by protein kinase A (PKA) in vivo on several residues of its amino terminus. Nevertheless, the PKA phosphorylation of Clast4 appeared to have no effect on either its eIF4E-binding ability or localization. Clast4 interacted with eIF4E1 and CPEB. The conserved eIF4E-binding sequence in Clast4, $YXXXXL_{\phi}$, was important for binding eIF4E1A but not eIF4E1B. Similar to that of another well-known eIF4E regulator, the eIF4E binding protein (4E-BP), the overexpression of Clast4 decreased cell proliferation. These results suggest that Clast4 acts as a global translation regulator in cells.

Translation Initiation Factor 4E (eIF4E) is Regulated by Cell Death Inhibitor, Diap1

  • Lee, Sun Kyung;Lee, Ji Sun;Shin, Ki Soon;Yoo, Soon Ji
    • Molecules and Cells
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    • v.24 no.3
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    • pp.445-451
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    • 2007
  • Translation initiation factor 4E (eIF4E) is a key regulator of protein synthesis. Abnormal regulation of eIF4E is closely linked to oncogenic transformation. Several regulatory mechanisms affecting eIF4E are discussed, including transcriptional regulation, phosphorylation and binding of an inhibitor protein. However it is not clear how the level of eIF4E protein is regulated under basal conditions. Here we demonstrate that Diap1 (Drosophila Inhibitor of Apoptosis Protein), a cell death inhibitor, binds directly to eIF4E and poly-ubiquitinates it via its E3 ligase activity, promoting its proteasome-dependent degradation. Expression of Diap1 caused a reduction of Cyclin D1 protein level and inhibited the growth stimulation induced by overexpression of eIF4E. Taken together, our results suggest that the level of eIF4E protein is regulated by Diap1, and that IAPs may play a role in cap-dependent translation by regulating the level of eIF4E protein.

Variability in the Viral Protein Linked to the Genome of Turnip Mosaic Virus Influences Interactions with eIF(iso)4Es in Brassica rapa

  • Li, Guoliang;Zhang, Shifan;Li, Fei;Zhang, Hui;Zhang, Shujiang;Zhao, Jianjun;Sun, Rifei
    • The Plant Pathology Journal
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    • v.37 no.1
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    • pp.47-56
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    • 2021
  • Plants protect against viruses through passive and active resistance mechanisms, and in most cases characterized thus far, natural recessive resistance to potyviruses has been mapped to mutations in the eukaryotic initiation factor eIF4E or eIF(iso)4E genes. Five eIF4E copies and three eIF(iso)4E copies were detected in Brassica rapa. The eIF4E and eIF(iso)4E genes could interact with turnip mosaic virus (TuMV) viral protein linked to the genome (VPg) to initiate virus translation. From the yeast two-hybrid system (Y2H) and bimolecular fluorescence complementation (BiFC) assays, the TuMV-CHN2/CHN3 VPgs could not interact with BraA.eIF4E.a/c or BraA.eIF(iso)4E.c, but they could interact with BraA.eIF(iso)4E.a in B. rapa. Further analysis indicated that the amino acid substitution L186F (nt T556C) in TuMV-UK1 VPg was important for the interaction networks between the TuMV VPg and eIF(iso)4E proteins. An interaction model of the BraA. eIF(iso)4E protein with TuMV VPg was constructed to infer the effect of the significant amino acids on the interaction of TuMV VPgs-eIF(iso)4Es, particularly whether the L186F in TuMV-UK1 VPg could change the structure of the TuMV-UK1 VPg protein, which may terminate the interaction of the BraA.eIF(iso)4E and TuMV VPg protein. This study provides new insights into the interactions between plant viruses and translation initiation factors to reveal the working of key amino acids.

EXTENSIONS OF GENERALIZED STABLE RINGS

  • Wanru, Zhang
    • Bulletin of the Korean Mathematical Society
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    • v.46 no.6
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    • pp.1091-1097
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    • 2009
  • In this paper, we investigate the extensions of generalized stable rings. It is shown that a ring R is a generalized stable ring if and only if R has a complete orthogonal set {e$_1$, . . . , e$_n$} of idempotents such that e$_1$Re$_1$, . . . , e$_n$Re$_n$ are generalized stable rings. Also, we prove that a ring R is a generalized stable ring if and only if R[[X]] is a generalized stable ring if and only if T(R,M) is a generalized stable ring.

Composite Hurwitz Rings Satisfying the Ascending Chain Condition on Principal Ideals

  • Lim, Jung Wook;Oh, Dong Yeol
    • Kyungpook Mathematical Journal
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    • v.56 no.4
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    • pp.1115-1123
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    • 2016
  • Let $D{\subseteq}E$ be an extension of integral domains with characteristic zero, I be a nonzero proper ideal of D and let H(D, E) and H(D, I) (resp., h(D, E) and h(D, I)) be composite Hurwitz series rings (resp., composite Hurwitz polynomial rings). In this paper, we show that H(D, E) satisfies the ascending chain condition on principal ideals if and only if h(D, E) satisfies the ascending chain condition on principal ideals, if and only if ${\bigcap}_{n{\geq}1}a_1{\cdots}a_nE=(0)$ for each infinite sequence $(a_n)_{n{\geq}1}$ consisting of nonzero nonunits of We also prove that H(D, I) satisfies the ascending chain condition on principal ideals if and only if h(D, I) satisfies the ascending chain condition on principal ideals, if and only if D satisfies the ascending chain condition on principal ideals.

Mutational Analyses of Translation Initiation Factor eIF1A in Saccharomyces cerevisiae (Saccharomyces cerevisiae에서 번역 개시 인자 eIF1A 돌연변이에 대한 분석)

  • Kwon, Sung-Hun;Kim, Jun-Ho;Choi, Bo-Kyung;Kim, Na-Yeon;Choi, Do-Hee;Park, Kyoung-Jun;Eoh, Jung-Hyun;Bae, Sung-Ho
    • Korean Journal of Microbiology
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    • v.45 no.3
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    • pp.239-245
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    • 2009
  • Translation initiation factor eIF1A performs essential functions in various initiation steps including 43S preinitiation complex formation in eukaryotes, and contains a highly conserved oligonucleotide-binding (OB) fold. In our previous study, we discovered that eIF1A possesses RNA annealing activity and forms a stable complex with double-stranded RNA. In this study, we initiated site-directed mutations in eIF1A to find the active sites for these biochemical activities and to investigate whether they are essential functions for yeast cell growth. A truncated protein, eIF1A($\Delta$T), devoid of both N- and C-terminal domains but containing an intact OB-fold exhibited RNA annealing activity. In contrast, all point mutations in OB-fold domain, except R57D, impaired both RNA annealing and dsRNA binding activities, indicating that the intact OB-fold domain is required for both activities. Viabilities of the mutant yeast cells were not correlated with RNA annealing activity but with the in vivo protein stabilities in the case of R57D and K94D.

ON THE PETTIS INTEGRABILITY

  • Kim, Jin Yee
    • Journal of the Chungcheong Mathematical Society
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    • v.8 no.1
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    • pp.111-117
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    • 1995
  • A function $f:{\Omega}{\rightarrow}X$ is called intrinsically-separable valued if there exists $E{\in}{\Sigma}$ with ${\mu}(E)=0$ such that $f({\Omega}-E)$ is a separable in X. For a given Dunford integrable function $f:{\Omega}{\rightarrow}X$ and a weakly compact operator T, we show that if f is intrinsically-separable valued, then f is Pettis integrable, and if there exists a sequence ($f_n$) of Dunford integrable and intrinsically-separable valued functions from ${\Omega}$ into X such that for each $x^*{\in}X^*$, $x^*f_n{\rightarrow}x^*f$ a.e., then f is Pettis integrable. We show that a function f is Pettis integrable if and only if for each $E{\in}{\Sigma}$, F(E) is $weak^*$-continuous on $B_{X*}$ if and only if for each $E{\in}{\Sigma}$, $M=\{x^*{\in}X^*:F(E)(x^*)=O\}$ is $weak^*$-closed.

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Construction and Characterization of Vector Expressing Low Level of Translation Factor eIF5B (단백질합성인자 eIF5B의 저 발현 효모벡터의 제조 및 특성)

  • 최상기;송진희;이준행;이병욱;성치남
    • Korean Journal of Microbiology
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    • v.40 no.1
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    • pp.7-11
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    • 2004
  • eIF5B is a translation initiation factor that delivers Met-$tRNA^{Met}$ to AUG start codon and subsequently joins the small and large ribosomes. In order to study the function of eIF5B encoded by FUN12, we constructed FUN12 which lacked 5' end of its sequence. We found that this construct lacking almost all of its promoter in pRS plasmid partially complemented slow growth phenotype of fun12 deletion strain. Interestingly, this construct expressed N-terminally truncated eIF5B and its expression level was about 5% of that of wild type eIF5B. Low amount of the eIF5B expressed additionally in fun12 deletion strain played a direct role as a limiting factor for its growth. This limiting factor eIF5B in those strains also modulates activities of overall translation in vitro.

EXTREMELY MEASURABLE SUBALGEBRAS

  • Ayyaswamy, S.K.
    • Bulletin of the Korean Mathematical Society
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    • v.22 no.1
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    • pp.7-10
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    • 1985
  • For each a.mem.S and f.mem.m(S), denote by $l_{a}$ f(s)=f(as) for all s.mem.S. If A is a norm closed left translation invariant subalgebra of m(S) (i.e. $l_{a}$ f.mem.A whenever f.mem.A and a.mem.S) containing 1, the constant ont function on S and .phi..mem. $A^{*}$, the dual of A, then .phi. is a mean on A if .phi.(f).geq.0 for f.geq.0 and .phi.(1) = 1, .phi. is multiplicative if .phi. (fg)=.phi.(f).phi.(g) for all f, g.mem.A; .phi. is left invariant if .phi.(1sf)=.phi.(f) for all s.mem.S and f.mem.A. It is well known that the set of multiplicative means on m(S) is precisely .betha.S, the Stone-Cech compactification of S[7]. A subalgebra of m(S) is (extremely) left amenable, denoted by (ELA)LA if it is nom closed, left translation invariant containing contants and has a multiplicative left invariant mean (LIM). A semigroup S is (ELA) LA, if m(S) is (ELA)LA. A subset E.contnd.S is left thick (T. Mitchell, [4]) if for any finite subser F.contnd.S, there exists s.mem.S such that $F_{s}$ .contnd.E or equivalently, the family { $s^{-1}$ E : s.mem.S} has finite intersection property.y.

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