신장인자

Ef-Tu(파란색), tRNA(빨간색), GTP(노란색)의 삼원 복합체. 출처: 2006년 9월 PDB Molecule of the Month 신장인자.

신장인자(伸長因子, 영어: elongation factor)는 단백질 합성 중에 기능하며, 신장하는 폴리펩타이드의 첫 번째 펩타이드 결합 형성부터 마지막 펩타이드 결합 형성까지 번역 과정에서의 신장을 촉진하는 단백질의 세트이다. 원핵생물에서 가장 흔한 신장인자는 EF-Tu, EF-Ts, EF-G이다.[1] 세균진핵생물은 서로 크게 상동적이지만 구조와 명명법이 다른 신장인자를 사용한다.[2]

신장은 번역에서 가장 빠른 단계이다.[3] 세균에서는 초당 15~20개의 아미노산(초당 약 45~60개의 뉴클레오타이드)이 첨가되는 속도로 진행된다. 진핵생물에서는 초당 약 2개의 아미노산(초당 약 6개의 뉴클레오타이드)이 첨가되는 속도로 진행된다. 신장인자는 이러한 과정들을 조절하고, 빠른 속도에서도 높은 정확도의 번역을 유지하는 역할을 담당한다.

상동적인 신장인자의 명명법

신장인자
세균 진핵생물/고세균 기능
EF-Tu eEF-1A (α)[2] 아미노아실-tRNA리보솜의 A 자리로 들어가는 것을 매개한다.[4]
EF-Ts eEF-1B (βγ)[2] EF-Tu에 대한 구아닌 뉴클레오타이드 교환인자로 작용하여 EF-Tu로부터 GDP의 방출을 촉매한다.[2]
EF-G eEF-2 각 단계의 폴리펩타이드의 신장시 리보솜에서 tRNA와 mRNA의 전위를 촉매한다. 입체형태의 변화를 크게 일으킨다.[5]
EF-P eIF-5A 아마도 펩타이드 결합의 형성을 자극하고 막힘을 해소한다.[6]
EF-4 (없음) 교정
EF-P의 고세균 및 진핵생물에서의 상동체인 EIF5A는 개시인자로 명명되었지만 이제는 신장인자로도 간주된다.[6]

진핵생물은 세포질의 번역 체계 외에도 미토콘드리아색소체에 독자적인 번역 체계를 가지고 있으며, 이들 세포소기관의 번역 체계는 세균의 것과 유사하다.[7][8] 사람의 경우 TUFM, TSFM, GFM1, GFM2, GUF1이 해당된다. 명목상의 방출인자MTRFR도 신장에 역할을 할 수 있다.[9]

세균에서 셀레노시스테이닐-tRNA는 EF-Tu와 관련된 특수 신장인자인 SelB (P14081)를 필요로 한다. 몇몇 동족체도 고세균에서 발견되지만, 기능은 알려져 있지 않다.[10]

표적

일부 병원체의 독소는 신장인자를 표적으로 한다. 예를 들어 독소형 디프테리아균(Corynebacterium diphtheriae)은 신장인자(EF-2)를 불활성화하여 숙주의 단백질 기능을 변경하는 디프테리아 독소를 생성한다. 이것은 디프테리아와 관련된 병리 및 증상을 초래한다. 마찬가지로 녹농균(Pseudomonas aeruginosa)의 외독소 A는 EF-2를 불활성화시킨다.[11]

같이 보기

각주

  1. Parker, J. (2001). 〈Elongation Factors; Translation〉. 《Encyclopedia of Genetics》. 610–611쪽. doi:10.1006/rwgn.2001.0402. ISBN 9780122270802. 
  2. Sasikumar, Arjun N.; Perez, Winder B.; Kinzy, Terri Goss (July 2012). “The Many Roles of the Eukaryotic Elongation Factor 1 Complex”. 《Wiley Interdisciplinary Reviews. RNA》 3 (4): 543–555. doi:10.1002/wrna.1118. ISSN 1757-7004. PMC 3374885. PMID 22555874. 
  3. Prabhakar, Arjun; Choi, Junhong; Wang, Jinfan; Petrov, Alexey; Puglisi, Joseph D. (July 2017). “Dynamic basis of fidelity and speed in translation: Coordinated multistep mechanisms of elongation and termination”. 《Protein Science》 26 (7): 1352–1362. doi:10.1002/pro.3190. ISSN 0961-8368. PMC 5477533. PMID 28480640. 
  4. Weijland A, Harmark K, Cool RH, Anborgh PH, Parmeggiani A (March 1992). “Elongation factor Tu: a molecular switch in protein biosynthesis”. 《Molecular Microbiology》 6 (6): 683–8. doi:10.1111/j.1365-2958.1992.tb01516.x. PMID 1573997. 
  5. Jørgensen, R; Ortiz, PA; Carr-Schmid, A; Nissen, P; Kinzy, TG; Andersen, GR (May 2003). “Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase.”. 《Nature Structural Biology》 10 (5): 379–85. doi:10.1038/nsb923. PMID 12692531. S2CID 4795260. 
  6. Rossi, D; Kuroshu, R; Zanelli, CF; Valentini, SR (2013). “eIF5A and EF-P: two unique translation factors are now traveling the same road.”. 《Wiley Interdisciplinary Reviews. RNA》 5 (2): 209–22. doi:10.1002/wrna.1211. PMID 24402910. S2CID 25447826. 
  7. Manuell, Andrea L; Quispe, Joel; Mayfield, Stephen P; Petsko, Gregory A (2007년 8월 7일). “Structure of the Chloroplast Ribosome: Novel Domains for Translation Regulation”. 《PLOS Biology》 5 (8): e209. doi:10.1371/journal.pbio.0050209. PMC 1939882. PMID 17683199. 
  8. G C Atkinson; S L Baldauf (2011). “Evolution of elongation factor G and the origins of mitochondrial and chloroplast forms”. 《Molecular Biology and Evolution》 28 (3): 1281–92. doi:10.1093/molbev/msq316. PMID 21097998. 
  9. “KEGG DISEASE: Combined oxidative phosphorylation deficiency”. 《www.genome.jp》. 
  10. Atkinson, Gemma C; Hauryliuk, Vasili; Tenson, Tanel (2011년 1월 21일). “An ancient family of SelB elongation factor-like proteins with a broad but disjunct distribution across archaea”. 《BMC Evolutionary Biology》 11 (1): 22. doi:10.1186/1471-2148-11-22. PMC 3037878. PMID 21255425. 
  11. Lee H, Iglewski WJ (1984). “Cellular ADP-ribosyltransferase with the same mechanism of action as diphtheria toxin and Pseudomonas toxin A”. 《Proc. Natl. Acad. Sci. U.S.A.》 81 (9): 2703–7. Bibcode:1984PNAS...81.2703L. doi:10.1073/pnas.81.9.2703. PMC 345138. PMID 6326138. 

더 읽을거리

  • Alberts, B. et al. (2002). Molecular Biology of the Cell, 4th ed. New York: Garland Science. ISBN 0-8153-3218-1.
  • Berg, J. M. et al. (2002). Biochemistry, 5th ed. New York: W.H. Freeman and Company. ISBN 0-7167-3051-0.
  • Singh, B. D. (2002). Fundamentals of Genetics, New Delhi, India: Kalyani Publishers. ISBN 81-7663-109-4.

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