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The evolution of ATPase activity in SMC proteins
Author(s) -
Cobbe Neville,
Heck Margarete M.S.
Publication year - 2006
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20795
Subject(s) - condensin , atp hydrolysis , atpase , cohesin , biology , microbiology and biotechnology , aaa proteins , function (biology) , computational biology , biochemistry , genetics , chromatin , enzyme , dna
The SMC ( s tructural m aintenance of c hromosomes) proteins are a highly conserved and ubiquitous family of ATPases, found in nearly all living organisms examined, where they play crucial roles in transmission of the hereditary material. However, the extent to which efficient ATP hydrolysis is required for SMC function has been a matter of some debate. Here we investigate the potential functional significance of ATP binding and hydrolysis in different eukaryotic SMC proteins, both by comparing the conservation of conserved ATPase motifs and by exploring potential coevolution between associated domains. In this way, we have been able to account for the reduced requirement for ATPase activity in cohesin's SMC3 and demonstrate the greater apparent conservation requirements for such activity in condensin SMC proteins. Finally, we explore possible interactions between the SMC and non‐SMC components of the condensin complex that are required for full condensin activity and may modulate ATPase activity in the holocomplex. Proteins 2006. © 2006 Wiley‐Liss, Inc.