scholarly journals Chlorella virus DNA ligase: Nick recognition and mutational analysis

1998 ◽  
Vol 26 (2) ◽  
pp. 502-531 ◽  
Author(s):  
V. Sriskanda ◽  
S. Shuman
Keyword(s):  
Mutational Analysis ◽  
Dna Ligase ◽  
Chlorella Virus

scholarly journals Solution NMR Studies of Chlorella Virus DNA Ligase-adenylate

2010 ◽  
Vol 395 (2) ◽  
pp. 291-308 ◽  
Author(s):  
Andrea Piserchio ◽  
Pravin A. Nair ◽  
Stewart Shuman ◽  
Ranajeet Ghose
Keyword(s):  
Solution Nmr ◽  
Dna Ligase ◽  
Nmr Studies ◽  
Chlorella Virus

scholarly journals Efficient DNA ligation in DNA–RNA hybrid helices by Chlorella virus DNA ligase

2013 ◽  
Vol 42 (3) ◽  
pp. 1831-1844 ◽  
Author(s):  
Gregory J. S. Lohman ◽  
Yinhua Zhang ◽  
Alexander M. Zhelkovsky ◽  
Eric J. Cantor ◽  
Thomas C. Evans
Keyword(s):  
Dna Ligase ◽  
Chlorella Virus ◽  
Dna Ligation

scholarly journals Characterization of an ATP-dependent DNA ligase encoded by Chlorella virus PBCV-1.

1997 ◽  
Vol 71 (3) ◽  
pp. 1931-1937 ◽  
Author(s):  
C K Ho ◽  
J L Van Etten ◽  
S Shuman
Keyword(s):  
Dna Ligase ◽  
Chlorella Virus

scholarly journals Mutations of the Yku80 C Terminus and Xrs2 FHA Domain Specifically Block Yeast Nonhomologous End Joining

2005 ◽  
Vol 25 (24) ◽  
pp. 10782-10790 ◽  
Author(s):  
Phillip L. Palmbos ◽  
James M. Daley ◽  
Thomas E. Wilson
Keyword(s):  
Mutational Analysis ◽  
Strand Break ◽  
Nonhomologous End Joining ◽  
Dna Ligase ◽  
End Joining ◽  
Fha Domain ◽  
Dna Ligase Iv ◽  
C Terminus ◽  
Ligase Iv ◽  
Two Hybrid

ABSTRACT The nonhomologous end-joining (NHEJ) pathway of DNA double-strand break repair requires three protein complexes in Saccharomyces cerevisiae: MRX (Mre11-Rad50-Xrs2), Ku (Ku70-Ku80), and DNA ligase IV (Dnl4-Lif1-Nej1). Much is known about the interactions that mediate the formation of each complex, but little is known about how they act together during repair. A comprehensive yeast two-hybrid screen of the NHEJ factors of S. cerevisiae revealed all known interactions within the MRX, Ku, and DNA ligase IV complexes, as well as three additional, weaker interactions between Yku80-Dnl4, Xrs2-Lif1, and Mre11-Yku80. Individual and combined deletions of the Yku80 C terminus and the Xrs2 forkhead-associated (FHA) domain were designed based on the latter two-hybrid results. These deletions synergistically blocked NHEJ but not the telomere and recombination functions of Ku and MRX, confirming that these protein regions are functionally important specifically for NHEJ. Further mutational analysis of Yku80 identified a putative C-terminal amphipathic α-helix that is both required for its NHEJ function and strikingly similar to a DNA-dependent protein kinase interaction motif in human Ku80. These results identify a novel role in yeast NHEJ for the poorly characterized Ku80 C-terminal and Xrs2 FHA domains, and they suggest that redundant binding of DNA ligase IV facilitates completion of this DNA repair event.

scholarly journals Functional Dynamics in Chlorella virus DNA Ligase

2009 ◽  
Vol 96 (3) ◽  
pp. 322a
Author(s):  
Andrea Piserchio ◽  
Pravin A. Nair ◽  
Stewart Stewart Shuman ◽  
Ranajeet Ghose
Keyword(s):  
Dna Ligase ◽  
Chlorella Virus ◽  
Functional Dynamics

scholarly journals Bacteriophage origin of some minimal ATP-dependent DNA ligases: a new structure from Burkholderia pseudomallei with striking similarity to Chlorella virus ligase

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Jolyn Pan ◽  
Kjersti Lian ◽  
Aili Sarre ◽  
Hanna-Kirsti S. Leiros ◽  
Adele Williamson
Keyword(s):  
Burkholderia Pseudomallei ◽  
Sequence Similarity ◽  
Structural Similarity ◽  
Striking Similarity ◽  
Leader Peptide ◽  
Dna Ligase ◽  
Genomic Context ◽  
Dna Ligases ◽  
Chlorella Virus ◽  
And Function

AbstractDNA ligases, the enzymes responsible for joining breaks in the phosphodiester backbone of DNA during replication and repair, vary considerably in size and structure. The smallest members of this enzyme class carry out their functions with pared-down protein scaffolds comprising only the core catalytic domains. Here we use sequence similarity network analysis of minimal DNA ligases from all biological super kingdoms, to investigate their evolutionary origins, with a particular focus on bacterial variants. This revealed that bacterial Lig C sequences cluster more closely with Eukaryote and Archaeal ligases, while bacterial Lig E sequences cluster most closely with viral sequences. Further refinement of the latter group delineates a cohesive cluster of canonical Lig E sequences that possess a leader peptide, an exclusively bacteriophage group of T7 DNA ligase homologs and a group with high similarity to the Chlorella virus DNA ligase which includes both bacterial and viral enzymes. The structure and function of the bacterially-encoded Chlorella virus homologs were further investigated by recombinantly producing and characterizing, the ATP-dependent DNA ligase from Burkholderia pseudomallei as well as determining its crystal structure in complex with DNA. This revealed that the enzyme has similar activity characteristics to other ATP-dependent DNA ligases, and significant structural similarity to the eukaryotic virus Chlorella virus including the positioning and DNA contacts of the binding latch region. Analysis of the genomic context of the B. pseudomallei ATP-dependent DNA ligase indicates it is part of a lysogenic bacteriophage present in the B. pseudomallei chromosome representing one likely entry point for the horizontal acquisition of ATP-dependent DNA ligases by bacteria.

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