• 제목/요약/키워드: translation regulation

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SR Proteins: Binders, Regulators, and Connectors of RNA

  • Jeong, Sunjoo
    • Molecules and Cells
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    • 제40권1호
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    • pp.1-9
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    • 2017
  • Serine and arginine-rich (SR) proteins are RNA-binding proteins (RBPs) known as constitutive and alternative splicing regulators. As splicing is linked to transcriptional and post-transcriptional steps, SR proteins are implicated in the regulation of multiple aspects of the gene expression program. Recent global analyses of SR-RNA interaction maps have advanced our understanding of SR-regulated gene expression. Diverse SR proteins play partially overlapping but distinct roles in transcription-coupled splicing and mRNA processing in the nucleus. In addition, shuttling SR proteins act as adaptors for mRNA export and as regulators for translation in the cytoplasm. This mini-review will summarize the roles of SR proteins as RNA binders, regulators, and connectors from transcription in the nucleus to translation in the cytoplasm.

Local protein synthesis in neuronal axons: why and how we study

  • Kim, Eunjin;Jung, Hosung
    • BMB Reports
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    • 제48권3호
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    • pp.139-146
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    • 2015
  • Adaptive brain function and synaptic plasticity rely on dynamic regulation of local proteome. One way for the neuron to introduce new proteins to the axon terminal is to transport those from the cell body, which had long been thought as the only source of axonal proteins. Another way, which is the topic of this review, is synthesizing proteins on site by local mRNA translation. Recent evidence indicates that the axon stores a reservoir of translationally silent mRNAs and regulates their expression solely by translational control. Different stimuli to axons, such as guidance cues, growth factors, and nerve injury, promote translation of selective mRNAs, a process required for the axon's ability to respond to these cues. One of the critical questions in the field of axonal protein synthesis is how mRNA-specific local translation is regulated by extracellular cues. Here, we review current experimental techniques that can be used to answer this question. Furthermore, we discuss how new technologies can help us understand what biological processes are regulated by axonal protein synthesis in vivo.

Saccharomyces cerevisiae에서 산화환원에 의한 In Vitro 단백질합성의 Thioredoxin에 중재된 조절 (Thioredoxin-Mediated Regulation of Protein Synthesis by Redox in Saccharomyces cerevisiae)

  • 최상기
    • 한국미생물·생명공학회지
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    • 제35권1호
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    • pp.36-40
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    • 2007
  • Redox signaling은 단백질을 산화환원 시키는 세포의 중요 신호가 전달되어, 그 단백질의 기능이 변화함으로써 세포의 성장 및 사멸을 조절하게 되는 과정이다. 단백질 합성 구성원의 산화, 환원 과정에 의한 단백질 합성 조절을 알아보기 위해 환원제인 DTT 존재 하에 단백질 합성 활성을 관찰한 결과 DTT가 존재하지 않는 것에 비해 단백질합성이 1.4배 정도 증가됨이 관찰되어 redox potential을 보이는 것으로 보아 환원제가 단백질 합성을 좀 더 증진시키는 것으로 사료된다. DTT에 의한 이러한 현상은 산화환원 조절 단백질인 thioredoxin를 첨가한다면 thiol기에 환원력이 전달되어 단백질합성이 더욱 촉진되기 때문에 효모에서 thioredoxin유전자를 cloning하고 이로부터 효모에서 GST-thioredoxin을 분리하였다. DTT 존재 하에 산화환원 조절 단백질인 thioredoxin을 농도별로 첨가하였을 때의 단백질 합성이 어떻게 조절되는지 알아보았다. 반응 액에 DTT를 넣은 것과 넣지 않은 것을 사용하여 thioredoxin을 0ng, 18ng, 90ng, 460ng, 2,300 ng의 농도로 각각 넣어서 반응시켜 보았다. 이렇게 반응시킨 반응물에서 만들어진 단백질 활성을 측정하였는데 thioredoxin의 농도가 높아질수록 그 활성이 높게 나타났으며, thioredoxin을 넣은 것이 넣지 않은 것에 비해 활성이 약 4배 이상 높게 나왔다 이 결과는 산화환원 조절 단백질인 thioredoxin이 환원력을 단백질합성구성원에 효율적으로 전달하는데 관여함을 보여주는 것이며, 산화환원이 단백질 합성 시 중요한 신호전달 과정임을 암시한다.

신경세포 연접후 위치에 단백질합성 해석시작인자(eIF)들의 존재 (Localization of Translation Initiation Factors to the Postsynaptic Sites)

  • 최명권;박성동;박인식;문일수
    • 생명과학회지
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    • 제21권11호
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    • pp.1526-1531
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    • 2011
  • 신경세포의 연접후 위치에서 단백질합성은 국소적 연접가소성의 조절에 중요한 역할을 한다. 본 연구에서는 연접후 위치에 eIF들이 존재하는지를 배양한 흰쥐해마신경세포의 면역세포화학적 염색과 immunoblot, 그리고 세제세척실험으로 알아보았다. 단백질해석 시작단계의 초기에 중요한 역할을 하는 eIF4E와 eIF4G, 개시코돈을 찾는 단계에서 중요한 eIF5, 외부자극에 의하여 합성을 시작하게 하는 eIF6, 그리고 불리한 환경에서 해석의 효율을 높여주는 eIF5A 들은 모두 해마신경세포의 연접후에 위치함을 배양한 해마신경세포를 다중초점형광현미경으로 관찰할 수 있었다. 또한 Immunoblot 실험에서도 이들은 연접후치밀질(PSD) 분획에서 검출되었으며, 여러 가지 세제에 의하여 PSD로부터 잘 떨어지지 않는 것으로 보아 PSD와 강하게 결합하고 있음을 알 수 있었다. 본 연구결과는 여러 가지 eIF들이 연접후에 위치하여 다양한 상황에서 단백질합성을 시작하게 할 수 있음을 시사한다.

Comparison of structure, function and regulation of plant cold shock domain proteins to bacterial and animal cold shock domain proteins

  • Chaikam, Vijay;Karlson, Dale T.
    • BMB Reports
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    • 제43권1호
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    • pp.1-8
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    • 2010
  • The cold shock domain (CSD) is among the most ancient and well conserved nucleic acid binding domains from bacteria to higher animals and plants. The CSD facilitates binding to RNA, ssDNA and dsDNA and most functions attributed to cold shock domain proteins are mediated by this nucleic acid binding activity. In prokaryotes, cold shock domain proteins only contain a single CSD and are termed cold shock proteins (Csps). In animal model systems, various auxiliary domains are present in addition to the CSD and are commonly named Y-box proteins. Similar to animal CSPs, plant CSPs contain auxiliary C-terminal domains in addition to their N-terminal CSD. Cold shock domain proteins have been shown to play important roles in development and stress adaptation in wide variety of organisms. In this review, the structure, function and regulation of plant CSPs are compared and contrasted to the characteristics of bacterial and animal CSPs.

Molecular Regulation of Pyrimidine Nucleotide Synthesis in Bacterial Genomes

  • Ghim, Sa-Youl
    • 한국미생물생명공학회:학술대회논문집
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    • 한국미생물생명공학회 2001년도 Proceedings of 2001 International Symposium
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    • pp.165-168
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    • 2001
  • Regulation of pyrimidine nucleotide synthesis has been studied extensively in enteric bacteria and Bacillus species. Varieties of control modes have been proposed for regulation of pyrimidine nucleotide biosynthetic (pyr) genes. In Bacillus caldolyticus and B. subtilis, it has been proved that pyrimidine de novo biosynthetic operon is controlled by a regulatory protein PyrR-mediated attenuation. Another Gram-positive bacteria including Enterococcus faecalis, Lactobacillus plantarum, and wctococcus lactis have been found to constitute a pyr gene cluster containing the pyrR gene. In addition, it has been proposed that the structure of the 5' leader region of the Gram-negative extreme thermophile Thermus strain Z05 pyr operon provides a novel mechanism of PyrR-dependent coupled transcription-translation attenuation. Bacterial genome sequencing projects have identified the PyrR homologues in Haemophilus influenzae, Synechocystis sp., Mycobacterium tuberculosis, Streptococcus pneumoniae, S. pyogenes, and Clostridium acetobutylicum, which are currently investigating for their physiological functions.

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노랑초파리의 $\alpha$-Glycerol-3-phosphate Dehydrogenase (GPDH)의 발현과 조절 (Regulation and Expression of Glycerol-3-phosphate Dehydrogerlase (GPDH) in Drosophila melanogaster)

  • 김세재;이정주남궁용김경진
    • 한국동물학회지
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    • 제34권1호
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    • pp.123-130
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    • 1991
  • Several parameters of u -glycerol-3-pholphate dehydrogenase (GPDH) such as activity, content and translatable mRNA levels were measured to elucidate mechanism underlving developmental and tissue specific regulation of 6PDH activity in Drosophila melonogastrr. In adult segments, most of total GPDH activity (62%1 Iwas detected in thorax where GPDH-1 resided, while 32% of total GPDH aUiviD was only detected in abdomen where GPDH-3 resided. The relative synthesis of GPDH was, however, similar in both tissues, although 58% of total GPDH was synthesized in abdomen. These results strongly suggest that the turnover rate of the abdominal enzyme (GPDH-3) was much more rapid than that of thoracic enzymes (GPDH-1). In nitro translation and immunoblotting experiments also indicate that GPDH-3 was arised by posttranslational modification from a single polypeptide (GPDH-1).

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Regulation of skeletal muscle protein synthesis by amino acid and resistance exercise

  • Nakai, Naoya
    • 운동영양학회지
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    • 제15권4호
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    • pp.153-161
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    • 2011
  • The maintenance of skeletal muscle mass is very important for the prevention of life style-related diseases and the improvement of quality of life. It is well-known that resistance exercise and nutrition (especially amino acids) are the most effective interventions for maintaining skeletal muscle mass. It has been reported that many molecules are involved in the regulation of protein synthesis in response to resistance exercise and nutrition. Understanding the molecular mechanisms regulating muscle protein synthesis is crucial for the development of appropriate interventions. The role of intracellular signaling pathways through the mammalian target of rapamycin (mTOR), a serine/threonine protein kinase in the regulation of muscle protein synthesis, has been extensively investigated for these years. Control of protein synthesis by mTOR is mediated through phosphorylation of downstream targets that modulate translation initiation and elongation step. In contrast, upstream mediators regulating mTOR and protein synthesis in response to resistance exercise and amino acid still needed to be determined. In this brief review, we discuss the current progress of intracellular mechanisms for exercise- and amino acid-induced activation of mTOR pathways and protein synthesis in skeletal muscle.

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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    • 제37권1호
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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.

Role of histone deacetylase 2 and its posttranslational modifications in cardiac hypertrophy

  • Eom, Gwang Hyeon;Kook, Hyun
    • BMB Reports
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    • 제48권3호
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    • pp.131-138
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    • 2015
  • Cardiac hypertrophy is a form of global remodeling, although the initial step seems to be an adaptation to increased hemodynamic demands. The characteristics of cardiac hypertrophy include the functional reactivation of the arrested fetal gene program, where histone deacetylases (HDACs) are closely linked in the development of the process. To date, mammalian HDACs are divided into four classes: I, II, III, and IV. By structural similarities, class II HDACs are then subdivided into IIa and IIb. Among class I and II HDACs, HDAC2, 4, 5, and 9 have been reported to be involved in hypertrophic responses; HDAC4, 5, and 9 are negative regulators, whereas HDAC2 is a pro-hypertrophic mediator. The molecular function and regulation of class IIa HDACs depend largely on the phosphorylation-mediated cytosolic redistribution, whereas those of HDAC2 take place primarily in the nucleus. In response to stresses, posttranslational modification (PTM) processes, dynamic modifications after the translation of proteins, are involved in the regulation of the activities of those hypertrophy-related HDACs. In this article, we briefly review 1) the activation of HDAC2 in the development of cardiac hypertrophy and 2) the PTM of HDAC2 and its implications in the regulation of HDAC2 activity.