http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
N4SSB 단백질의 C-말단기의 7개의 아미노산이 N4SSB 단백질의 in vivo 활성에 미치는 영향
최미영,Choi, Mieyoung 한국미생물학회 1998 미생물학회지 Vol.34 No.4
Bacteriophage N4, a lytic phage specific for Esherichia coli K12 strain encodes single-stranded DNA-binding protein, N4SSB (bacteriophage N4-coded single-stranded DNA-binding protein). N4SSB protein is originally identified as a protein required for N4 DNA replication. N4SSB protein is also required for N4 late transcription, which is catalyzed by E. coli ${\sigma}^{70}$ RNA polymerase. N4 late transcription does not occur until N4SSB protein is synthesized. Recently it is reported that N4SSB protein is essential for N4 DNA recombination. Therefore N 4SSB protein is a multifunctional protein required for N4 DNA replication, late transcription, and N4 DNA recombination. In this study, a variety of mutant N4SSB proteins containing internal deletions or substitutions were constructed to define and characterize domains important for N4 DNA replication, late transcription, and N4 DNA recombination. Test for the ill vivo activity of these mutant N4SSBs for N4 DNA replication, late transcription, and N4 DNA recombination was examined. The results suggest that C-terminal 7 amino acid residues are important for the activity of N4SSB. Three lysine residues, which are contained in this region play important roles on N4SSB activity. Esherichia coli(E. coli) K12 균주를 숙주세포로 삼는 박테리오파아지인 N4는 single-stranded DNA에 결합하는 단백질인 N4SSB(bacteriophage N4-coded single-stranded DNA-binding protein) 단백질을 만든다. N4SSB 단백질은 N4 DNA replication 뿐만 아니라 late transcription과 N4 DNA recombination에도 필요한 여러 가지 기능을 가진 단백질이다. N4 late transcription은 숙주세포인 E. coli의 $E{\sigma}^{70}$ RNA polymerase에 의해서 수행이 되나 N4SSB 단백질을 반드시 필요로 하기 때문에 N4SSB 단백질이 생성될 때까지는 N4 late promoter로부터 RNA 합성이 일어나지 않는다. 본 연구에서는 N4SSB의 N4 DNA replication과 late transcription, 그리고 N4 DNA recombination에 필요한 영역(domain)을 알아내기 위해서 여러 가지 돌연변이형 N4SSB 단백질을 만들어 N4 DNA replication과 late transcription, 그리고 N4 DNA recombination의 3가지 작용에 대한 in vivo 활성을 조사 분석하였다. 그 결과 N4SSB 단백질의 C-말단기에 있는 7개의 아미노산이 N4SSB 단백질의 활성에 중요하다는 것을 알 수 있었다. 특히 C-말단기의 7개의 아미노산에는 세 개의 lysine이 포함되어 있는데 이 lysine이 N4SSB 단백질의 활성에 중요한 역할을 한다는 것이 제시되었다.
Jeong, Haeng-Soon,Jeong, In-Chel,Kim, Andre,Kang, Shin-Won,Kang, Ho Sung,Kim, Yung-Jin,Lee, Suk-Hee,Park, Jang-Su 부산대학교 유전공학연구소 2002 분자생물학 연구보 Vol.18 No.-
Eukaryotic replication protein A (RPA) is a single-stranded(ss) DNA binding protein with multiple functions in DNA replication, repair, and genetic recombination. The 70-kDa subunit of eukaryotic RPA contains a conserved four cysteine-type zinc-finger motif that has been implicated in the regulation of DNA replication and repair. Recently, we described a novel function for the zine-finger motif in the regulation of human RPA's ssDNA binding activity through reduction-oxidation (redox). Here, we show that yeast RPA's ssDNA binding activity is regulated by redox potential through its RPA32 and/or RPA14 subunits. Yeast RPA requires a reducing agent, such as dithiothreitol (DTT), for its ssDNA binding activity. Also, under non-reducing conditions, its DNA binding activity decreases 20 fold. In contrast, the RPA70 subunit does not require DTT for its DNA binding activity and is not affected by the redox condition. These results suggest that all three subunits are required for the regulation of RPA's DNA binding activity through redox potential.
Jeong, Haeng-Soon,Jeong, In-Chel,Kim, Andre,Kang, Shin-Won,Kang, Ho-Sung,Kim, Yung-Jin,Lee, Suk-Hee,Park, Jang-Su Korean Society for Biochemistry and Molecular Biol 2002 Journal of biochemistry and molecular biology Vol.35 No.2
Eukaryotic replication protein A (RPA) is a single-stranded(ss) DNA binding protein with multiple functions in DNA replication, repair, and genetic recombination. The 70-kDa subunit of eukaryotic RPA contains a conserved four cysteine-type zinc-finger motif that has been implicated in the regulation of DNA replication and repair. Recently, we described a novel function for the zinc-finger motif in the regulation of human RPA's ssDNA binding activity through reduction-oxidation (redox). Here, we show that yeast RPA's ssDNA binding activity is regulated by redox potential through its RPA32 and/or RPA14 subunits. Yeast RPA requires a reducing agent, such as dithiothreitol (DTT), for its ssDNA binding activity. Also, under non-reducing conditions, its DNA binding activity decreases 20 fold. In contrast, the RPA 70 subunit does not require DTT for its DNA binding activity and is not affected by the redox condition. These results suggest that all three subunits are required for the regulation of RPA's DNA binding activity through redox potential.
김안드레,박장수 한국분자세포생물학회 2002 Molecules and cells Vol.13 No.3
The eukaryotic replication protein A (RPA) is a heterotrimeric protein complex. It consists of 70, 32, and 14 kDa subunits that are involved in DNA replication, repair, and genetic recombination. RPA is a 4-cysteine type zinc-finger protein. RPA’s zinc-finger domain is not essential for DNA binding activity, but it is involved in the regulation of RPA’s DNA binding activity through reduction-oxidation (redox). In this study, we show that yeast RPA’s ssDNA binding activity is regulated by redox potential through its subcomplexes of 32 and 14 kDa subunits. In contrast, the subunits’ complex, RPA70, formed a stable complex with ssDNA, even under non-reducing conditions. The addition of DTT and H2O2 had no effect on its DNA binding activity. In RPA70, since the addition of the subcomplexes of the 32 and 14 kDa subunits, it restored the modulating ssDNA binding activity to native RPA’s DNA binding activity. These results suggest that the subcomplexes of the 32 and 14 kDa subunits may be involved in the modulating RPA’s DNA binding activity through redox change. These studies, therefore, show the novel structure and function relationship of a multiprotein complex in that the role of a specific domain (or one subunit) is regulated by the other subunits.
( Mi-ra Choi ),( Jung-min Shin ),( Young-ah Shin ),( Yun-hee Chang ),( Min-youl Chang ),( Cho-ah Lim ),( Kyung-cheol Sohn ),( Young-joon Seo ),( Chang-deok Kim ),( Jeung-hoon Lee ),( Young Lee ) 대한피부과학회 2018 Annals of Dermatology Vol.30 No.4
Background: Skin hydration is a common problem both in elderly and young people as dry skin may cause irritation, dermatological disorders, and wrinkles. While both genetic and environmental factors seem to influence skin hydration, thorough genetic studies on skin hydration have not yet been conducted. Objective: We used a genome-wide association study (GWAS) to explore the genetic elements underlying skin hydration by regulating epidermal differentiation and skin barrier function. Methods: A GWAS was conducted to investigate the genetic factors influencing skin hydration in 100 Korean females along with molecular studies of genes in human epidermal keratinocytes for functional study in vitro. Results: Among several single nucleotide polymorphisms identified in GWAS, we focused on Single Stranded DNA Binding Protein 3 (SSBP3) which is associated with DNA replication and DNA damage repair. To better understand the role of SSBP3 in skin cells, we introduced a calcium-induced differentiation keratinocyte culture system model and found that SSBP3 was upregulated in keratinocytes in a differentiation dependent manner. When SSBP3 was overexpressed using a recombinant adenovirus, the expression of differentiation-related genes such as loricrin and involucrin was markedly increased. Conclusion: Taken together, our results suggest that genetic variants in the intronic region of SSBP3 could be determinants in skin hydration of Korean females. SSBP3 represents a new candidate gene to evaluate the molecular basis of the hydration ability in individuals. (Ann Dermatol 30(4) 432∼440, 2018)