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N-α-아세틸전달효소10

N-alpha-acetyltransferase 10
NAA10
식별자
에일리어스NAA10, ARD1, ARD1A, ARD1P, DXS707, MCOPS1, NATD, TE2, OGDNS, N(alpha)-아세틸전달효소 10, NatA 촉매서브유닛, HARD1, N-alpha-아세틸전달효소 10, NatA 촉매서브유닛
외부 IDOMIM: 300013 MGI: 1915255 HomoloGene: 2608 GenCard: NAA10
맞춤법
종.인간마우스
엔트레즈

8260

56292

앙상블

ENSG00000102030

ENSMUSG000031388

유니프로트

P41227

Q9QY36

RefSeq(mRNA)

NM_003491
NM_001256119
NM_001256120

NM_001177965
NM_019870
NM_001310538

RefSeq(단백질)

NP_001243048
NP_001243049
NP_003482

NP_001171436
NP_001297467
NP_063923

장소(UCSC)Chr X: 153.93 ~153.94 MbChr X: 72.96 ~72.97 Mb
PubMed 검색[3][4]
위키데이터
인간 보기/편집마우스 표시/편집

N-α-아세틸전달효소 10(NAA10)은 NatA 촉매 서브유닛 Naa10 및 구속결핍 단백질 1 호몰로 A(ARD1A)라고도 하며, 인체에서 NAA10 유전자를 [5][6]코드하는 효소 서브유닛이다.Naa10은 보조 서브유닛 Naa15와 함께 특정 단백질의 아세틸-CoA에서 N말단 1차 아미노기로의 아세틸기 전달을 특이적으로 촉매하는 NatA(N-아세틸전달효소α A) 착체를 구성한다.고등 진핵생물에서는 N-아세틸전달효소(NAT) 복합체 NatB-NatF가 기재특이성과 서브유닛 [7]조성 모두 다르다.

유전자 및 기록

인간 NAA10은 Xq28 염색체에 위치하며 8개의 엑손과 2개의 엑손이 번갈아 스플라이싱에서 [8]파생된 3개의 다른 아이소폼을 코드한다.또한 여러 인간 [9]세포주 내에서 발현되는 NAA10 유전자 복제 NAA11(ARD2)이 확인되었지만, 이후 연구에 따르면 Naa11은 인간 세포주 HeLa 및 HEK293 또는 암 조직 내에서 발현되지 않으며 NAA11 전사물은 고환 및 태반 [10]조직에서만 검출되었다.Naa11은 주로 [11]고환에서 발현되는 생쥐에서도 발견되었다.NAA11은 사람의 경우 4q21.21 염색체에, 생쥐의 경우 5개의 E3 염색체에 위치하며, 2개의 엑손만 포함한다.생쥐들은 또 다른 Naa10과 비슷한 패럴로그인 Naa12를 가지고 있다.Naa12는 NAT 활성을 가지며 Naa10의 손실을 유전적으로 보상하지만 Naa10/Naa12 늘은 마이크에서 태아 치사량입니다.[12]

마우스에서 NAA10은 X A7.3 염색체에 위치하며 9개의 엑손이 포함되어 있다.마우스 Naa10의 두 가지 대체 스플라이싱 생성물인 mNaa10과235 mNaa10은225 서로 다른 세포 하위 [13]구획에서 서로 다른 활성과 기능을 가질 수 있는 NIH-3T3와 JB6 세포에서 보고되었다.

Naa10에 대한 호몰로그는 식물,[14][15][16] 곰팡이,[14][17] 아메보조아,[14] 고세균[14][18][19][20],[21][22] 원생동물을 포함한 분석된 거의 모든 생물 왕국에서 확인되었다.유박테리아에서는 RimI, RimJ, RimL 등 3가지 N-아세틸전달효소가α 확인되었으나 NATs와의[23][24][25] 낮은 배열 동일성에 따르면 RIM 단백질이 공통 조상을 가지지 않고 독립적으로 [26][27]진화했을 가능성이 높다.

구조.

크기 제외 크로마토그래피와 원형 이색성에 따르면 인간 Naa10은 단백질의 3분의 2로 이루어진 콤팩트한 구상 영역과 유연한 비구조화 [28]C-말단으로 구성되어 있다.S. pombe의 100 kD 홀로-NatA 복합체(Naa10/Naa15)의 X선 결정 구조는 Naa10이 하나의 큰 소수성 인터페이스를 특징으로 하는 전형적인 GNAT 접힘을 채택하고 보조 소단위 Naa15, 중앙 아세틸 CO-결합 영역과 상호작용을 보이는 것으로 나타났다.또 다른 N-아세틸전달효소인α [29]Naa50의 해당 부위에 유사하다.고고 T. 화산 Naa10의 X선 결정 구조도 보고되었으며, P-루프를 [20]포함한 β4와 α3 사이의 루프를 포함하는 여러 가지 다른 아세틸-Co 결합 모드가 밝혀졌다.비착체(Naa15 결합) Naa10은 Leu22 및 Tyr26이 Naa10의 활성부위 밖으로 시프트하고, Glu24(NatA의 기판결합 및 촉매에 중요)가 약 5Ω 위치하여 다른 [29]서브셋의 아세틸화를 가능하게 하는 배치가 된다.Naa15 및 HYPK와 복합체인 인간 Naa10의 X선 결정 구조가 [30]보고되었다.

잔류물 78과 83(KRSR) 사이의 hNaa10의 C 말단에서의 기능적 핵국재신호가 [31][32]기술되었다.

기능.

Naa10은 NatA 착체의 일부로서 개시제 메티오닌(iMet)이 메티오닌아미노펩티다아제(MetAP)[33]에 의해 분해된 후 리보솜에 결합되어 Ser, Ala, Thr, Glie, Val 및 Cys 등의 작은 측쇄에서 시작하여 단백질을 공역적으로 아세틸화한다.또한 비리보솜 관련 Naa10에 의한 번역 후 아세틸화가 발생할 수 있다.모든 단백질의 약 40~50%는 잠재적 NatA [7][34]기질이다.또, 단량체 상태에서는, 기판 결합 포켓 Naa10의 구조 재배치에 의해, 산성의 측쇄에 [29][35]의한 N-termini의 아세틸화를 가능하게 한다.또한 N-아세틸전달효소ε 활성[36][37][38][39][40][41][42] 및 N-말단 프로피오닐전달효소 활성도 보고되었다.

단백질의α N 말단 아세틸화가 수년간 알려져 왔음에도 불구하고, 이러한 수정의 기능적 결과는 잘 알려져 있지 않다.하지만, 증거를 축적하는 다양한 신호 경로에, Wnt[38][39][44][45]MAPK,[44]JAK[46]과 NF-κB,[47][48][49][50] 다양한 휴대 프로세스 조절 등 세포 migration,[51][52]세포 주기 control,[53][54][55]DNA손상 control,[49][56]caspase-dependent 세포 death,[56][57]포함 Naa10과 연관 짓고 있다.P53종속 apoptosis,[54]세포 확산과autophagy[58]뿐만 아니라 hypo.비록 [39][40][42][59][60]저산소증에[61][62][63][64][65] 관한 몇 가지 주요한 불일치가 있지만 Naa10 기능의 Isoform 특이적 효과는 [13][66]마우스에서 보고되었다.

Naa10은 D. melanogaster,[67] C. elegans[68],[21] T. brucei에 필수적입니다.S. cerevisiae에서는 Naa10 기능이 필수적이지 않지만 yNAA10Ω 세포는 사일런트 결합형 궤적(HML)의 디억제, G상 진입o 실패, 온도 감도, 성장 [17][69]저하 등 심각한 결함을 보인다.Naa10 녹아웃 생쥐가 생존 가능한 것으로 보고되어 뼈 [50]발달에 결함이 있는 것으로 나타났다.

질병

2001년 A c.109T > C(p).NAA10의 Ser37Pro) 변종은 Ogden Syndrome(오그덴 증후군)와 관련이 없는 두 개의 가족에서 확인되었으며, Ogden Syndrome(오그덴 증후군)은 노화된 외모, 두개 안면 이상, 저혈압, 전지구적 발달 지연, 크립토르키디즘,[70] 심장 부정맥의 뚜렷한 조합을 수반한다.환자 섬유아세포는 변형된 형태학, 성장 및 이동 특성을 보였으며 분자 연구 결과 이러한 S37P 돌연변이가 NatA 복합체를 교란시키고 체외 및 [70][71][72]체내 Naa10 효소 활성을 감소시키는 것으로 나타났다.

또한 Naa10의 두 가지 다른 돌연변이(남자아이의 R116W 돌연변이 및 여자아이의 V107F 돌연변이)는 비동색성 지적장애, 산발적 성장부전 및 골격 이상 [73][74]증례를 가진 두 개의 관련 없는 가족에서 기술되었다.소녀는 폰타넬 폐쇄 지연, 골연령 지연, 넓은 엄지발가락, 가벼운 펙투스 카리나툼, 폐동맥협착증, 심방중격결손, QT간격연장 등으로 알려졌다.그 소년은 작은 손발, 높은 아치형 입천장, 넓은 치간 공간을 가지고 있는 것으로 보고되었다.

또한 NAA10의 인트론7 스플라이스 공여부위(c.471+2T→A)의 스플라이스 돌연변이(splice 돌연변이)는 매우 드물고 유전적으로 이질적인 X-연결 열성 장애인 Lensz Microphalmia syndrome(LMS)를 가진 단일 패밀리에서 보고되었다.치아, 손가락,[75] 발가락의 기형환자 섬유아세포는 세포 증식 결함, STRA6와 같은 레티노인산 시그널링 경로에 관여하는 유전자의 조절 장애, 레티놀 [75]흡수 부족 등을 보였다.

축적된 증거는 Naa10 기능이 샤페론 기능 변조를 통해 동시 번역 단백질 접힘을 조절하여 알츠하이머병에서 독성 아밀로이드 응집체의 병리학적 형성과 [76][77][78][79]효모에서 프리온 [PSI+] 증식에 영향을 줄 수 있음을 시사한다.

NAA10 관련 신드롬에 대한 자세한 내용은 www.naa10gene.com를 참조하십시오.

메모들

레퍼런스

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추가 정보

외부 링크

  • PDB의 UniProt: P41227(N-alpha-acetyl transferase 10)에 있는 PDB의 모든 구조 정보의 개요.