Evidence for binary Smc complexes lacking kite subunits in archaea
SMC complexes play a central role in chromosome organization in all domains of life. The bacterial Smc–ScpAB complex is a three-subunit complex composed of Smc, ScpA and ScpB. ScpA bridges the two ATPase domains of the Smc homodimer, while ScpB, which belongs to the kite family of proteins, interact...
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| Format: | Article |
| Language: | English |
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International Union of Crystallography
2020-03-01
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| Series: | IUCrJ |
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| Online Access: | http://scripts.iucr.org/cgi-bin/paper?S2052252519016634 |
| _version_ | 1798025797626232832 |
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| author | Jae-Hyun Jeon Han-Sol Lee Ho-Chul Shin Mi-Jeong Kwak Yeon-Gil Kim Stephan Gruber Byung-Ha Oh |
| author_facet | Jae-Hyun Jeon Han-Sol Lee Ho-Chul Shin Mi-Jeong Kwak Yeon-Gil Kim Stephan Gruber Byung-Ha Oh |
| author_sort | Jae-Hyun Jeon |
| collection | DOAJ |
| description | SMC complexes play a central role in chromosome organization in all domains of life. The bacterial Smc–ScpAB complex is a three-subunit complex composed of Smc, ScpA and ScpB. ScpA bridges the two ATPase domains of the Smc homodimer, while ScpB, which belongs to the kite family of proteins, interacts with ScpA. The three subunits are known to be equally important for the function of Smc–ScpAB in bacteria. From crystallographic and biochemical studies, evidence is provided that six archaeal ScpA proteins are unable to interact with the only putative ScpB found in these species. Structure-based sequence alignment reveals that these archaeal ScpAs lack the ScpB-binding segment that is commonly present in the middle of bacterial ScpA sequences, which is thus responsible for their inability to interact with ScpB. ScpA proteins lacking the ScpB-binding segment are found to prevail in archaea. Moreover, two archaeal ScpA proteins with a longer middle region also failed to bind their putative ScpB partner. Furthermore, all or most species belonging to five out of 14 euryarchaeotal orders contain Smc and ScpA but not a detectable ScpB homologue. These data support the notion that archaeal Smc-based complexes generally function as a two-subunit complex composed of only Smc and ScpA. |
| first_indexed | 2024-04-11T18:24:34Z |
| format | Article |
| id | doaj.art-d304442392634d89982df100a346e305 |
| institution | Directory Open Access Journal |
| issn | 2052-2525 |
| language | English |
| last_indexed | 2024-04-11T18:24:34Z |
| publishDate | 2020-03-01 |
| publisher | International Union of Crystallography |
| record_format | Article |
| series | IUCrJ |
| spelling | doaj.art-d304442392634d89982df100a346e3052022-12-22T04:09:40ZengInternational Union of CrystallographyIUCrJ2052-25252020-03-017219320610.1107/S2052252519016634be5282Evidence for binary Smc complexes lacking kite subunits in archaeaJae-Hyun Jeon0Han-Sol Lee1Ho-Chul Shin2Mi-Jeong Kwak3Yeon-Gil Kim4Stephan Gruber5Byung-Ha Oh6Department of Biological Science, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of KoreaDepartment of Biological Science, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of KoreaDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, Republic of KoreaCKD Research Institute, ChongKunDang Pharmaceutical Corp., Yongin, Gyeonggi 16995, Republic of KoreaPohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, Kyungbuk 37673, Republic of KoreaDepartment of Fundamental Microbiology, University of Lausanne, Bâtiment Biophore, 1015 Lausanne, SwitzerlandDepartment of Biological Science, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of KoreaSMC complexes play a central role in chromosome organization in all domains of life. The bacterial Smc–ScpAB complex is a three-subunit complex composed of Smc, ScpA and ScpB. ScpA bridges the two ATPase domains of the Smc homodimer, while ScpB, which belongs to the kite family of proteins, interacts with ScpA. The three subunits are known to be equally important for the function of Smc–ScpAB in bacteria. From crystallographic and biochemical studies, evidence is provided that six archaeal ScpA proteins are unable to interact with the only putative ScpB found in these species. Structure-based sequence alignment reveals that these archaeal ScpAs lack the ScpB-binding segment that is commonly present in the middle of bacterial ScpA sequences, which is thus responsible for their inability to interact with ScpB. ScpA proteins lacking the ScpB-binding segment are found to prevail in archaea. Moreover, two archaeal ScpA proteins with a longer middle region also failed to bind their putative ScpB partner. Furthermore, all or most species belonging to five out of 14 euryarchaeotal orders contain Smc and ScpA but not a detectable ScpB homologue. These data support the notion that archaeal Smc-based complexes generally function as a two-subunit complex composed of only Smc and ScpA.http://scripts.iucr.org/cgi-bin/paper?S2052252519016634smcscpascpbarchaeakite proteinssmc–scpasmc–scpabcondensin |
| spellingShingle | Jae-Hyun Jeon Han-Sol Lee Ho-Chul Shin Mi-Jeong Kwak Yeon-Gil Kim Stephan Gruber Byung-Ha Oh Evidence for binary Smc complexes lacking kite subunits in archaea IUCrJ smc scpa scpb archaea kite proteins smc–scpa smc–scpab condensin |
| title | Evidence for binary Smc complexes lacking kite subunits in archaea |
| title_full | Evidence for binary Smc complexes lacking kite subunits in archaea |
| title_fullStr | Evidence for binary Smc complexes lacking kite subunits in archaea |
| title_full_unstemmed | Evidence for binary Smc complexes lacking kite subunits in archaea |
| title_short | Evidence for binary Smc complexes lacking kite subunits in archaea |
| title_sort | evidence for binary smc complexes lacking kite subunits in archaea |
| topic | smc scpa scpb archaea kite proteins smc–scpa smc–scpab condensin |
| url | http://scripts.iucr.org/cgi-bin/paper?S2052252519016634 |
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