diplomsko delo
Abstract
Spojitveni faktor, bogat s prolini in glutamini (SFPQ), je protein, ki lahko interagira tako
s proteini kot tudi z RNA in DNA. Posledično sodeluje pri mnogih procesih v celici in
ima vse večji pomen v raziskavah, ki so povezane z nevrodegenerativnimi boleznimi. Cilj
diplomske naloge je bil izraziti in izolirati protein SFPQ v taki količini in čistosti, ki bi
omogočila nadaljnje eksperimente, npr. spremljanje nastanka parapeg in vitro. Pripravili
smo vektorja pMCSG7-MBP-SFPQ (N-končna fuzija z MBP in His6) in pMCSG7-SFPQ
(SFPQ brez fuzij). SFPQ smo nato izražali z izhodiščnim vektorjem pJ4M-SFPQ-MBP
in z vektorjem pMCSG7-MBP-SFPQ. Fuzija s His6 je omogočila izolacijo proteina s
pomočjo afinitetne kromatografije z imobiliziranimi kovinskimi ioni (IMAC). Konstrukt
SFPQ-MBP se je razgradil že med izražanjem. MBP-SFPQ se je izražal v dovolj velikih
količinah, a je pri postopkih izolacije prišlo do razgradnje. Z vektorjem pMCSG7-SFPQ
smo izražali SFPQ brez fuzij in ga izolirali z dodatkom cinkovega klorida. Do proteolize
je prišlo pri izražanju in/ali izolaciji. Sklepali smo, da je vzrok za razgradnjo proteina
velik delež neurejene strukture, ki je zato bolj občutljiv na proteaze. Postopke bi morali
optimizirati in zmanjšati aktivnost proteaz.
Keywords
spojitveni faktor, bogat s prolini in glutamini;protein SFPQ;izražanje;amiotrofična lateralna skleroza;ALS;frontotemporalna demenca;FTD;diplomska dela;
Data
Language: |
Slovenian |
Year of publishing: |
2023 |
Typology: |
2.11 - Undergraduate Thesis |
Organization: |
UL FKKT - Faculty of Chemistry and Chemical Technology |
Publisher: |
[A. Pervanja] |
UDC: |
577.21:577.112(043.2) |
COBISS: |
164612355
|
Views: |
16 |
Downloads: |
3 |
Average score: |
0 (0 votes) |
Metadata: |
|
Other data
Secondary language: |
English |
Secondary title: |
Cloning and expression of the protein SFPQ |
Secondary abstract: |
Splicing factor proline and glutamine rich (SFPQ) is a protein that interacts with protein,
RNA and DNA. Because of that, it has a plethora of cell functions and is increasingly
popular among neurodegenerative disease studies. Our aim was to express and purify
enough SFPQ to conduct experiments such as monitoring the formation of paraspeckles.
Vectors pMCSG7-MBP-SFPQ (N-terminal fusion with MBP and His6) and pMCSG7-
SFPQ (untagged SFPQ) were prepared. SFPQ was then expressed using pJ4M-SFPQMBP
(prepared in the lab) and pMCSG7-MBP-SFPQ vectors. The fusion with His6
allowed the protein to be purified by immobilized metal ion affinity chromatography
(IMAC). SFPQ-MBP was already degraded during expressing. MBP-SFPQ was
expressed in sufficient amounts, but degradation occurred during the purification steps.
We used the pMCSG7-SFPQ vector to express untagged SFPQ and isolate it by adding
zinc chloride. Proteolysis occurred upon expression and/or purification. We concluded
that the cause of protein degradation is a large proportion of the disordered structure,
which is more sensitive to proteases. The procedures should therefore be optimized to
reduce the activity of proteases. |
Secondary keywords: |
SEPQ;expressing;ALS;FTD;Beljakovine;Nevrodegenerativne bolezni;Molekularno kloniranje;Univerzitetna in visokošolska dela; |
Type (COBISS): |
Bachelor thesis/paper |
Study programme: |
1000371 |
Embargo end date (OpenAIRE): |
1970-01-01 |
Thesis comment: |
Univ. v Ljubljani, Fak. za kemijo in kemijsko tehnologijo, UNI Biokemija |
Pages: |
38 str. |
ID: |
19909001 |