Loading...
Please wait, while we are loading the content...
Similar Documents
A thermophilic phage uses a small terminase protein with a fixed helix–turn–helix geometry
| Content Provider | Scilit |
|---|---|
| Author | Hayes, Janelle A. Hilbert, Brendan J. Gaubitz, Christl Stone, Nicholas P. Kelch, Brian A. |
| Copyright Year | 2020 |
| Description | Journal: Journal of Biological Chemistry Tailed bacteriophages use a DNA-packaging motor to encapsulate their genome during viral particle assembly. The small terminase (TerS) component of this DNA-packaging machinery acts as a molecular matchmaker that recognizes both the viral genome and the main motor component, the large terminase (TerL). However, how TerS binds DNA and the TerL protein remains unclear. Here we identified gp83 of the thermophilic bacteriophage P74-26 as the TerS protein. We found that $TerS^{P76-26}$ oligomerizes into a nonamer that binds DNA, stimulates TerL ATPase activity, and inhibits TerL nuclease activity. A cryo-EM structure of $TerS^{P76-26}$ revealed that it forms a ring with a wide central pore and radially arrayed helix–turn–helix domains. The structure further showed that these helix–turn–helix domains, which are thought to bind DNA by wrapping the double helix around the ring, are rigidly held in an orientation distinct from that seen in other TerS proteins. This rigid arrangement of the putative DNA-binding domain imposed strong constraints on how $TerS^{P76-26}$ can bind DNA. Finally, the $TerS^{P76-26}$ structure lacked the conserved C-terminal β-barrel domain used by other TerS proteins for binding TerL. This suggests that a well-ordered C-terminal β-barrel domain is not required for $TerS^{P76-26}$ to carry out its matchmaking function. Our work highlights a thermophilic system for studying the role of small terminase proteins in viral maturation and presents the structure of $TerS^{P76-26}$, revealing key differences between this thermophilic phage and its mesophilic counterparts. |
| Related Links | https://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=2662&context=faculty_pubs http://www.jbc.org/article/S0021925817487734/pdf |
| Ending Page | 3793 |
| Page Count | 11 |
| Starting Page | 3783 |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| DOI | 10.1074/jbc.ra119.012224 |
| Journal | Journal of Biological Chemistry |
| Issue Number | 12 |
| Volume Number | 295 |
| Language | English |
| Publisher | Elsevier BV |
| Publisher Date | 2020-03-01 |
| Access Restriction | Open |
| Subject Keyword | Journal: Journal of Biological Chemistry Biochemistry and Molecular Biology Dna-binding Protein Helix–turn–helix Domain |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
