• Bulletin of the Korean Chemical Society
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• 제20권10호
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• pp.1126-1128
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• 1999

• 미생물학회지
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• 제27권3호
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• pp.194-200
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• 1989

S. aureus에서 분리된 plasmid pSBK203 상의 CAT 유전자 염기서열을 결정하였으며 유발성 발현현상이 확인되었다. 염기서열 결과에 의해 예측된 단백질의 아미노산 서열 분석결고 pC221-CAT 와는 78%의 가장 높은 상동성을 나타냈으며 pC194-CAT와는 55%, 그람음성균 유래의 CAT 중 하나인 Tn9-CATdhkss 38%의 상동성을 각각 보여주고 있었다.

• 대한바이러스학회지
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• 제30권1호
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• pp.1-10
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• 2000

The nonstructural protein NSP4, encoded by gene 10 of rotavirus, has been shown to playa role in viral assembly and known to be an enterotoxin, causing diarrhea in mouse pups. NSP4 gene was cloned from CBNU-2 (virulent bovine rotavirus/diarrheic fecal sample) and CBNU-1 (cell-culture adapted bovine rotavirus/isolated from CBNU-2 and 75 times passaged on MA104 cells), respectively, by reverse transcriptase-polymerase chain reaction (RT-PCR) and sequenced and compared. The sequence data indicated that the NSP4 genes of bovine rotavirus (BRV) were 751 bases in length and encoded one open reading frame of 175 amino acids beginning at base 42 and terminating at base 569. Differences in nucleotide sequence between CBNU-2 and CBNU-1 were observed at 6 positions (base 274, 296, 391, 394, 396 and 579). NSP4 gene of BRV exhibited a high degree of nucleotide (90% and 94%) and amino acid sequence (91% and 97%) homology with those of SA11 and UK but a low degree of nucleotide (77% and 79%) and amino acids sequence (81% and 85%) homology with those of Wa and OSU.

• Parasites, Hosts and Diseases
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• 제41권2호
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• pp.129-133
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• 2003

A complete cDNA sequence encoding a pore-forming subunit (Kir6.2) of ATP-senstive potassium channel in the adult worm, Clonorchis sinensis, termed CsKir6.2, was isolated from an adult CDNA library. The cDNA contained a single open-reading frame of 333 amino acids, which has a structural motif (a GFG-motif) of the putative pore-forming loop of the Kir6.2. Peculiarly, the Cskir6.2 shows a lack-sequence structure, which deleted 57 amino acids were deleted from its N-terminus. The predicted amino acid sequence revealed a highly conserved sequence as other known other Kir6.2 subunits. The mRNA was weekly expressed in the adult worm.

• 미생물학회지
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• 제40권3호
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• pp.211-216
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• 2004

세포외 phospholipase D (PLD)를 과량 생산하는 균주 JE-11을 토양으로부터 분리하였다. 16S rDNA에 의한 분석과 형태적, 생리적 특성을 조사한 결과 이 균은 Streptomyces somaliensis로 동정되었다. 선발한 S. somaliensis로 부터 PLD를 암호화하는 유전자(sspld) 분리하고 염기서열을 조사하였다. Open reading frame을 분석한 결과 33개의 아미노산으로 이루어진 분비 signal peptide와 505개의 아미노산으로 구성된 PLD단백질을 암호화하는 것으로 예상되었다. 또한, sspld의 염기 서열로부터 유추된 단백질 서열은 기존에 보고된 다른 Streptomyces PLD들과 70-88％의 서열 유사성을 보였다. 이 PLD는 96-98％(㏖/㏖)의 수율로서, Phosphatidylcholine을 glycerol과 serine을 기질로 하여 각각 phosphatidylglycerol 과phosphatidylserine으로 전환을 하였으나, 알코올 공여체인 inositol과 ethanolamine과는 반응하지 않았다.

• Archives of Pharmacal Research
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• 제19권6호
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• pp.497-501
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• 1996

A gene coding for triosephosphate isomerase (TPI) from a rat skeletal muscle cDNA library was cloned and its nucleotide sequence was determined. The 1, 348-bp cDNA clone contains 24 bp $5^I$ noncoding region, the entire 750 bp coding region corresponding to a protein of 249 amino acids, $547bp 3^I$ noncoding region and part of a poly(A) tail. It also contains a polyadenylation signal, AATAAA, starting from 17 bp upstream of the poly(A) tail. The calculated molecular weight of rat TPI is 27.8 kDa and the net charge is +4. The deduced amino acid sequence from rat TPI CDNA sequence has 93% and 94% homology with that of mouse and human clones, respectively. The amino acids at the residue of Asn12, Lys14, His96, Glu 166, His96, His101, Ala177, Tyr165, Glu13O, Tyr2O9, and Ser212 in catalytic site are completely identical, confirming that the functional residues in TPI proteins are highly conserved throughout evolution. The most profound characteristic of rat TPI enzyme, compared with other TPIs, is that there are five cysteine substitutions at the residue of 21, 27, 159, 195 and 204. A Glu123 instead of Gly was found in rabbit, rhesus, mouse and human sequences. Through the method of RT-PCR, the mRNA transcription level of TPI gene was found to be different among various tissues and was highest in muscle.

• 정보처리학회논문지D
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• 제12D권1호
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• pp.51-62
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• 2005

하나의 아미노산 서열의 기능이 밝혀지면, 그와 유사한 서열 구조를 가지고 있는 서열의 기능도 유추해 낼 수 있다. 또한 기능이 밝혀진 단백질의 아미노산 서열을 변화시키거나 유용한 단백질을 만드는 것도 가능하다. 이 과정에서 하나의 원본 단백질 서열에 대하여 다른 서열 구성을 가지고 있는 여러 가지 단백질 서열이 생겨 날 수 있다. 여기서, 원본 단백질을 변화시켜 만든 단백질 버전 서열과 단백질의 주석정보를 저장 및 관리하는 체계적인 기법이 요구된다. 따라서 이 논문에서는 로컬 서열 정렬 기법을 적용한 단백질 아미노산 서열의 버전관리 기법과 트리거를 적용한 단백질 주석데이터의 이력 관리 기법을 제시하였다. 제안된 기법을 통하여 원본 서열과 버전서열의 유사도 측정 및 버전 관리의 자동화와 저장 공간을 감소시킬 수 있다. 또한 단백질 정보의 이력을 저장하고 서열 변화 정보를 분석하여 돌연변이 연구에 의한 유용한 단백질 개발 및 신약 개발이 가능하다.

• 약학회지
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• 제43권6호
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• pp.743-750
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• 1999

Human and bovine dopamine transporters (DAT) demonstrate discrete functional differences in the dopamine (DA) transport and cocaine binding. The functional analyses on the chimeras of human and bovine DAT have revealed that the region from the $133^{rd}{\;}to{\;}186^{th}$ residue(encompassing the $3^{rd}$ trans-membrane domain (TM) is responsible for the substrate transport and cocaine binding. The present studies have been done to find out the specific amino acid(s) which is essential for the binding of cocaine to DAT by interchanging the amino acids in that region between human and bovine DAT. When isoleucine, the $152^{nd}$ residue of chimera B3 (bovine DAT sequence) was transformed back to valine, the human DAT residue at the identical position, the cocaine binding was remarkably recovered to 98% of the human DAT values. In addition, the cocaine binding of the human DAT was decreased by 57% by substituting isoleucine for valine at position 152. When isoleucine at position 152 of the chimera B3 was converted to the other amino acids to provide an possible molecular basis for the functional role of the $152^{nd}$ residue, only the conversion to alanine among acids tested significantly the cocaine by 34%, but these effect were not as much as those by the conversion to valine. In conclusion, valine at position 152 is a crucial amino acid for the interaction of cocaine to the DAT.

• Journal of Microbiology and Biotechnology
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• 제5권3호
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• pp.117-124
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• 1995

A gene (xynA) encoding the endo-xylanase (E.C.3.2.1.8) from Bacillus stearothermophilus was cloned in E. coli, and its complete nucleotide sequence was determined. The xynA gene consists of a 636 base pairs open reading frame coding for a protein of 212 amino acids with a deduced molecular weight of 23, 283 Da. A putative signal sequence of 27 amino acid residues shows the features comparable with the Bacillus signal sequences; namely, the signal contains a positively charged region close to the N-terminus followed by a long hydrophobic string. The coding sequence is preceded by a possible ribosome binding site with a free energy value of -16.6 kcal/mol and the transcription initiation signals are located further upstream. The translation termination codon (TAA) at the 3 end of the coding sequence is followed by two palindrome sequences, one of which is thought to act as a terminator. The xynA gene has a high GC content, especially in the wobble position of codons (64%). Comparison of the primary protein sequence with those of other xylanases shows a high homology to the xylanases belonging to family G.

• Molecules and Cells
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• 제27권5호
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• pp.539-546
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• 2009

In Saccharomyces cerevisiae, ribosomal protein L7, one of the ~46 ribosomal proteins of the 60S subunit, is encoded by paralogous RPL7A and RPL7B genes. The amino acid sequence identity between RPl7a and RPl7b is 97 percent; they differ by only 5 amino acid residues. Interestingly, despite the high sequence homology, Rpl7b is detected in both the cytoplasm and the nucleolus, whereas Rpl7a is detected exclusively in the cytoplasm. A site-directed mutagenesis experiment revealed that the change in the amino acid sequence of Rpl7b does not influence its subcellular localization. In addition, introns of RPL7A and RPL7B did not affect the subcellular localization of Rpl7a and Rpl7b. Remarkably, Rpl7b was detected exclusively in the cytoplasm in rpl7a knockout mutant, and overexpression of Rpl7a resulted in its accumulation in the nucleolus, indicating that the subcellular localization of Rpl7a and Rpl7b is influenced by the intracellular level of Rpl7a. Rpl7b showed a wide range of localization patterns, from exclusively cytoplasmic to exclusively nucleolar, in knockout mutants for some rRNA-processing factors, nuclear pore proteins, and large ribosomal subunit assembly factors. Rpl7a, however, was detected exclusively in the cytoplasm in these mutants. Taken together, these results suggest that although Rpl7a and Rpl7b are paralogous and functionally replaceable with each other, their precise physiological roles may not be identical.