2017
KITE proteins: new insights to evolution and dynamics of SMC complexes
PALEČEK, Jan; Stephan GRUBER; Marek ADAMUS; Tomas KLUMPLER; Lucie VONDROVÁ et al.Základní údaje
Originální název
KITE proteins: new insights to evolution and dynamics of SMC complexes
Název anglicky
KITE proteins: new insights to evolution and dynamics of SMC complexes
Autoři
PALEČEK, Jan; Stephan GRUBER; Marek ADAMUS; Tomas KLUMPLER; Lucie VONDROVÁ; Katerina ZABRADY a Antony W OLIVER
Vydání
2nd meeting on SMC proteins: chromosomal organizers from bacteria to human, 2017
Další údaje
Typ výsledku
Vyžádané přednášky
Utajení
není předmětem státního či obchodního tajemství
Označené pro přenos do RIV
Ne
Změněno: 9. 8. 2017 16:39, doc. Mgr. Jan Paleček, Dr. rer. nat.
V originále
We described marked structural similarities between prokaryotic SMC/ScpAB, MukBEF and eukaryotic SMC5/6 complexes (Palecek and Gruber, Structure, 2015). They posses short kleisin molecules while condensin and cohesin complexes contain long kleisins. All kleisins bind SMC proteins through their conserved N- and C-terminal domains while their different middle regions associate with different types of subunits: short kleisins interact with KITE (Kleisin-Interacting Tandem winged-helix Element) and long klesins interact with HAWK (HEAT Associated With Kleisin) proteins. The presence of KITE proteins in prokaryotic SMC/ScpAB and eukaryotic SMC5/6 complexes suggests their close evolutionary relation and an evolutionary path from prokaryotic to eukaryotic SMC complexes via SMC5/6-like ancestors. Different structural features of the KITE and HAWK proteins suggest different regulation and mechanics of their respective SMC complexes. We will show KITE structural elements and their dynamic properties that might be involved in shaping of the kleisin molecules. We will propose a new KITE role in regulation of prokaryotic SMC/ScpAB and eukaryotic SMC5/6 complexes.
Anglicky
We described marked structural similarities between prokaryotic SMC/ScpAB, MukBEF and eukaryotic SMC5/6 complexes (Palecek and Gruber, Structure, 2015). They posses short kleisin molecules while condensin and cohesin complexes contain long kleisins. All kleisins bind SMC proteins through their conserved N- and C-terminal domains while their different middle regions associate with different types of subunits: short kleisins interact with KITE (Kleisin-Interacting Tandem winged-helix Element) and long klesins interact with HAWK (HEAT Associated With Kleisin) proteins. The presence of KITE proteins in prokaryotic SMC/ScpAB and eukaryotic SMC5/6 complexes suggests their close evolutionary relation and an evolutionary path from prokaryotic to eukaryotic SMC complexes via SMC5/6-like ancestors. Different structural features of the KITE and HAWK proteins suggest different regulation and mechanics of their respective SMC complexes. We will show KITE structural elements and their dynamic properties that might be involved in shaping of the kleisin molecules. We will propose a new KITE role in regulation of prokaryotic SMC/ScpAB and eukaryotic SMC5/6 complexes.
Návaznosti
| MUNI/M/0822/2015, interní kód MU |
|