Pregled bibliografske jedinice broj: 523228
Purification of enzymatically inactive peptidylarginine deiminase type 6 from mouse ovary that reveals hexameric structure different from other dimeric isoforms
Purification of enzymatically inactive peptidylarginine deiminase type 6 from mouse ovary that reveals hexameric structure different from other dimeric isoforms // Advances in bioscience and biotechnology, 2 (2011), 304-310 doi:10.4236/abb.2011.24044 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 523228 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Purification of enzymatically inactive peptidylarginine deiminase type 6 from mouse ovary that reveals hexameric structure different from other dimeric isoforms
Autori
Taki, Hirofumi ; Gomi, Tomoharu ; Knuckley, Bryan ; Thompson, R Paul ; Vugrek, Oliver ; Hirata, Kazuya ; Miyahara, Tatsurou ; Shinoda, Kouichiro ; Hounoki, Hiroyuki ; Sugiyama, Eiji ; Usui, Isao ; Urakaze, Masaharu ; Tobe, Kazuyuki ; Ishimoto, Tetsuya ; Inoue, Ran: Tanaka, Ayumi ; Mano, Hiroki ; Ogawa, Hirofumi ; Mori, Hisashi
Izvornik
Advances in bioscience and biotechnology (2156-8456) 2
(2011);
304-310
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
Peptidylarginine Deiminase ; Isoform ; Dimer ; Hexamer ; Mouse Oocytes ; Cytoplasmic Sheets
Sažetak
The murine peptidylarginine deiminase (PAD) has five isoforms encoded by different genes and partici- pates in a variety of cellular functions through the citrullination of target proteins. The crystal structure of human PAD4 with a dimeric form was previously solved because of the enzyme’s relevance to rheuma- toid arthritis. PAD6, abundant in mouse oocytes and eggs, is believed to take part in early events of embryogenesis, but its biochemical properties are little understood. Here we have purified and charac- terized a recombinant PAD6. A PAD6 cDNA was cloned from mouse ovary RNA and expressed in Escherichia coli through pET29 and pGEX vectors. When benzoyl-L-arginine ethyl ester was used as a substrate, no appreciable activity was detected with a cell homogenate under conditions where a human PAD4 cDNA caused significant activity. Both pro- teins were affinity-purified to near homogeneity. The circular dichroism spectra of PAD6 and human PAD4 were similar in the far ultraviolet region. On molecular sieving, PAD6 was eluted faster than human PAD4. The cross-linking of PAD6 with dime- thyl suberimidate clearly showed six bands on an sodium dodecyl sulfate-polyacrylamide gel. These results indicate that PAD6 can constitute a hexameric structure. The purified PAD6 still showed no enzy- matic activity. This unique structure and loss in enzymatic activity is strongly suggested to favor the formation of egg cytoplasmic sheets as the architectu- ral protein.
Izvorni jezik
Engleski
Znanstvena područja
Biologija, Temeljne medicinske znanosti, Biotehnologija
POVEZANOST RADA
Projekti:
098-0000000-2463 - Nedostatak Adenozilhomocistein hidrolaze: Molekularni mehanizmi novog oboljenja (Vugrek, Oliver, MZOS ) ( CroRIS)
Ustanove:
Institut "Ruđer Bošković", Zagreb
Profili:
Oliver Vugrek
(autor)
Citiraj ovu publikaciju:
Uključenost u ostale bibliografske baze podataka::
- CAB Abstracts
- The Library of Congress
- DOAJ
- CSP
- CrossRef
- Google Schoolar
- ProQuest
- Gale
- Nanjing University
- University of Science and Technology of China
- East China University of Science and Technology
- University of Electronic Science and Technology of China
- Beijing University of Civil Engineering and Architecture