Білковий сплайсинг


Білковий сплайсинг або сплайсинг білків є внутрішньомолекулярною реакцією деяких протеїнів, під час якої певна внутрішня ділянка поліпептидного ланцюга (так званий інтеїн) видаляє сама себе; в результаті фрагменти поліпептиду що залишились (так звані екстеїни) сполучаються між собою утворюючи новий, коротший білок. Зшивання екстеїнів як правило відбувається впритул до залишків цистеїну або серину (амінокислоти що містять нуклеофільний бічний ланцюг). Цей процес не вимагає екзогенних кофакторів або джерел енергії, таких як аденозинтрифосфат (АТФ) і гуанозинтрифосфат (ГТФ). 



Типи інтеїнів |


Інтеїни поділяють на чотири групи: максі-інтеїни, міні-інтеїни, транс-сплайсингові інтеїни, а також аланінові інтеїни. Максі-інтеїни мають в своєму складі домен ендонуклеази. Міні-інтеїни є меншими за довжиною і не мають ендонуклеаза домену. В транс-сплайсингових інтеїнах інтеїновий фрагмент розділений на два (або можливо більше) фрагментів, які входять до складу різних білкових доменів. Нарешті аланінові інтеїни мають лігуються по залишку аланіну, замість цистеїну або серину.



Історія відкриття |


Білковий сплайсинг був несподівано відикритий в 1990 році двома групами вчених які працювали незалежно, а саме групою Анраку (англ. Anraku) [1]
і групою Стівенса (англ. Stevens [2]). Обидві групи вивчали білок VMA1 в дріжжах Saccharomyces cerevisiae. 



Посилання |




  1. ↑ Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae. J. Biol. Chem. 265 (12). April 1990. с. 6726–33. PMID 2139027. 


  2. ↑ Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase. Science 250 (4981). November 1990. с. 651–7. PMID 2146742. doi:10.1126/science.2146742. 








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