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Article ; Online: P53 conformational switching for selectivity may reveal a general solution for specific DNA binding.

Tubbs, Julie L / Tainer, John A

2011 Volume 30, Issue 11, Page(s) 2099–2100

MeSH term(s)	DNA/metabolism ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; Humans ; Models, Biological ; Protein Binding ; Protein Conformation ; Tumor Suppressor Protein p53/chemistry ; Tumor Suppressor Protein p53/metabolism
Chemical Substances	DNA-Binding Proteins ; Tumor Suppressor Protein p53 ; DNA (9007-49-2)
Language	English
Publishing date	2011-06-01
Publishing country	England
Document type	Comment ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.1038/emboj.2011.133
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Article ; Online: Alkyltransferase-like proteins: molecular switches between DNA repair pathways.

Tubbs, Julie L / Tainer, John A

Cellular and molecular life sciences : CMLS

2010 Volume 67, Issue 22, Page(s) 3749–3762

Abstract: Alkyltransferase-like proteins (ATLs) play a role in the protection of cells from the biological effects of DNA alkylation damage. Although ATLs share functional motifs with the DNA repair protein and cancer chemotherapy target O⁶-alkylguanine-DNA ... ...

Abstract	Alkyltransferase-like proteins (ATLs) play a role in the protection of cells from the biological effects of DNA alkylation damage. Although ATLs share functional motifs with the DNA repair protein and cancer chemotherapy target O⁶-alkylguanine-DNA alkyltransferase, they lack the reactive cysteine residue required for alkyltransferase activity, so its mechanism for cell protection was previously unknown. Here we review recent advances in unraveling the enigmatic cellular protection provided by ATLs against the deleterious effects of DNA alkylation damage. We discuss exciting new evidence that ATLs aid in the repair of DNA O⁶-alkylguanine lesions through a novel repair cross-talk between DNA-alkylation base damage responses and the DNA nucleotide excision repair pathway.
MeSH term(s)	Amino Acid Sequence ; Animals ; DNA/chemistry ; DNA/metabolism ; DNA Repair ; Humans ; Models, Molecular ; Molecular Sequence Data ; O(6)-Methylguanine-DNA Methyltransferase/chemistry ; O(6)-Methylguanine-DNA Methyltransferase/metabolism ; Sequence Alignment ; Signal Transduction
Chemical Substances	DNA (9007-49-2) ; O(6)-Methylguanine-DNA Methyltransferase (EC 2.1.1.63)
Language	English
Publishing date	2010-05-26
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-010-0405-8
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Article: Alkyltransferase-like proteins: molecular switches between DNA repair pathways

Tubbs, Julie L / Tainer, John A

Cellular and molecular life sciences CMLS. 2010 Nov., v. 67, no. 22

2010

Abstract	Alkyltransferase-like proteins (ATLs) play a role in the protection of cells from the biological effects of DNA alkylation damage. Although ATLs share functional motifs with the DNA repair protein and cancer chemotherapy target O ⁶-alkylguanine-DNA alkyltransferase, they lack the reactive cysteine residue required for alkyltransferase activity, so its mechanism for cell protection was previously unknown. Here we review recent advances in unraveling the enigmatic cellular protection provided by ATLs against the deleterious effects of DNA alkylation damage. We discuss exciting new evidence that ATLs aid in the repair of DNA O ⁶-alkylguanine lesions through a novel repair cross-talk between DNA-alkylation base damage responses and the DNA nucleotide excision repair pathway.
Keywords	DNA repair
Language	English
Dates of publication	2010-11
Size	p. 3749-3762.
Publisher	SP Birkhäuser Verlag Basel
Publishing place	Basel
Document type	Article
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-010-0405-8
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Article: DNA binding, nucleotide flipping, and the helix-turn-helix motif in base repair by O6-alkylguanine-DNA alkyltransferase and its implications for cancer chemotherapy.

Tubbs, Julie L / Pegg, Anthony E / Tainer, John A

DNA repair

2007 Volume 6, Issue 8, Page(s) 1100–1115

Abstract: O(6)-Alkylguanine-DNA alkyltransferase (AGT) is a crucial target both for the prevention of cancer and for chemotherapy, since it repairs mutagenic lesions in DNA, and it limits the effectiveness of alkylating chemotherapies. AGT catalyzes the unique, ... ...

Abstract	O(6)-Alkylguanine-DNA alkyltransferase (AGT) is a crucial target both for the prevention of cancer and for chemotherapy, since it repairs mutagenic lesions in DNA, and it limits the effectiveness of alkylating chemotherapies. AGT catalyzes the unique, single-step, direct damage reversal repair of O(6)-alkylguanines by selectively transferring the O(6)-alkyl adduct to an internal cysteine residue. Recent crystal structures of human AGT alone and in complex with substrate DNA reveal a two-domain alpha/beta fold and a bound zinc ion. AGT uses its helix-turn-helix motif to bind substrate DNA via the minor groove. The alkylated guanine is then flipped out from the base stack into the AGT active site for repair by covalent transfer of the alkyl adduct to Cys145. An asparagine hinge (Asn137) couples the helix-turn-helix DNA binding and active site motifs. An arginine finger (Arg128) stabilizes the extrahelical DNA conformation. With this newly improved structural understanding of AGT and its interactions with biologically relevant substrates, we can now begin to unravel the role it plays in preserving genetic integrity and discover how it promotes resistance to anticancer therapies.
MeSH term(s)	Amino Acid Sequence ; Animals ; Catalytic Domain ; Crystallography, X-Ray ; DNA/chemistry ; DNA/metabolism ; DNA Modification Methylases/chemistry ; DNA Modification Methylases/genetics ; DNA Modification Methylases/metabolism ; DNA Repair ; DNA Repair Enzymes/chemistry ; DNA Repair Enzymes/genetics ; DNA Repair Enzymes/metabolism ; Drug Resistance, Neoplasm ; Helix-Turn-Helix Motifs ; Humans ; Models, Molecular ; Molecular Sequence Data ; Neoplasms/drug therapy ; Neoplasms/metabolism ; Nucleotides/chemistry ; O(6)-Methylguanine-DNA Methyltransferase/chemistry ; O(6)-Methylguanine-DNA Methyltransferase/genetics ; O(6)-Methylguanine-DNA Methyltransferase/metabolism ; Sequence Homology, Amino Acid ; Substrate Specificity ; Tumor Suppressor Proteins/chemistry ; Tumor Suppressor Proteins/genetics ; Tumor Suppressor Proteins/metabolism
Chemical Substances	Nucleotides ; Tumor Suppressor Proteins ; DNA (9007-49-2) ; DNA Modification Methylases (EC 2.1.1.-) ; MGMT protein, human (EC 2.1.1.63) ; O(6)-Methylguanine-DNA Methyltransferase (EC 2.1.1.63) ; DNA Repair Enzymes (EC 6.5.1.-)
Language	English
Publishing date	2007-08-01
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2071608-4
ISSN	1568-7856 ; 1568-7864
ISSN (online)	1568-7856
ISSN	1568-7864
DOI	10.1016/j.dnarep.2007.03.011
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Article: Crystallographic structures of Discosoma red fluorescent protein with immature and mature chromophores: linking peptide bond trans-cis isomerization and acylimine formation in chromophore maturation.

Tubbs, Julie L / Tainer, John A / Getzoff, Elizabeth D

Biochemistry

2005 Volume 44, Issue 29, Page(s) 9833–9840

Abstract: The mature self-synthesizing p-hydroxybenzylideneimidazolinone-like fluorophores of Discosoma red fluorescent protein (DsRed) and Aequorea victoria green fluorescent protein (GFP) are extensively studied as powerful biological markers. Yet, the ... ...

Abstract	The mature self-synthesizing p-hydroxybenzylideneimidazolinone-like fluorophores of Discosoma red fluorescent protein (DsRed) and Aequorea victoria green fluorescent protein (GFP) are extensively studied as powerful biological markers. Yet, the spontaneous formation of these fluorophores by cyclization, oxidation, and dehydration reactions of tripeptides within their protein environment remains incompletely understood. The mature DsRed fluorophore (Gln 66, Tyr 67, and Gly 68) differs from the GFP fluorophore by an acylimine that results in Gln 66 Calpha planar geometry and by a Phe 65-Gln 66 cis peptide bond. DsRed green-to-red maturation includes a green-fluorescing immature chromophore and requires a chromophore peptide bond trans-cis isomerization that is slow and incomplete. To clarify the unique structural chemistry for the individual immature "green" and mature "red" chromophores of DsRed, we report here the determination and analysis of crystal structures for the wild-type protein (1.4 A resolution), the entirely green DsRed K70M mutant protein (1.9 A resolution), and the DsRed designed mutant Q66M (1.9 A resolution), which shows increased red chromophore relative to the wild-type DsRed. Whereas the mature, red-fluorescing chromophore has the expected cis peptide bond and a sp(2)-hybridized Gln 66 Calpha with planar geometry, the crystal structure of the immature green-fluorescing chromophore of DsRed, presented here for the first time, reveals a trans peptide bond and a sp(3)-hybridized Gln 66 Calpha with tetrahedral geometry. These results characterize a GFP-like immature green DsRed chromophore structure, reveal distinct mature and immature chromophore environments, and furthermore provide evidence for the coupling of acylimine formation with trans-cis isomerization.
MeSH term(s)	Acylation ; Animals ; Anthozoa/chemistry ; Anthozoa/genetics ; Crystallization ; Crystallography, X-Ray ; Green Fluorescent Proteins/chemistry ; Hydrozoa ; Imines/chemistry ; Isomerism ; Luminescent Proteins/chemistry ; Luminescent Proteins/genetics ; Mutagenesis, Site-Directed ; Peptides/chemistry ; Peptides/genetics ; Red Fluorescent Protein
Chemical Substances	Imines ; Luminescent Proteins ; Peptides ; fluorescent protein 583 ; green fluorescent protein, Aequorea victoria ; Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2005-11-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi0472907
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Article ; Online: Repair of O4-alkylthymine by O6-alkylguanine-DNA alkyltransferases.

Fang, Qingming / Kanugula, Sreenivas / Tubbs, Julie L / Tainer, John A / Pegg, Anthony E

The Journal of biological chemistry

2009 Volume 285, Issue 11, Page(s) 8185–8195

Abstract: O(6)-Alkylguanine-DNA alkyltransferase (AGT) plays a major role in repair of the cytotoxic and mutagenic lesion O(6)-methylguanine (m(6)G) in DNA. Unlike the Escherichia coli alkyltransferase Ogt that also repairs O(4)-methylthymine (m(4)T) efficiently, ... ...

Abstract	O(6)-Alkylguanine-DNA alkyltransferase (AGT) plays a major role in repair of the cytotoxic and mutagenic lesion O(6)-methylguanine (m(6)G) in DNA. Unlike the Escherichia coli alkyltransferase Ogt that also repairs O(4)-methylthymine (m(4)T) efficiently, the human AGT (hAGT) acts poorly on m(4)T. Here we made several hAGT mutants in which residues near the cysteine acceptor site were replaced by corresponding residues from Ogt to investigate the basis for the inefficiency of hAGT in repair of m(4)T. Construct hAGT-03 (where hAGT sequence -V(149)CSSGAVGN(157)- was replaced with the corresponding Ogt -I(143)GRNGTMTG(151)-) exhibited enhanced m(4)T repair activity in vitro compared with hAGT. Three AGT proteins (hAGT, hAGT-03, and Ogt) exhibited similar protection from killing by N-methyl-N'-nitro-N-nitrosoguanidine and caused a reduction in m(6)G-induced G:C to A:T mutations in both nucleotide excision repair (NER)-proficient and -deficient Escherichia coli strains that lack endogenous AGTs. hAGT-03 resembled Ogt in totally reducing the m(4)T-induced T:A to C:G mutations in NER-proficient and -deficient strains. Surprisingly, wild type hAGT expression caused a significant but incomplete decrease in NER-deficient strains but a slight increase in T:A to C:G mutation frequency in NER-proficient strains. The T:A to C:G mutations due to O(4)-alkylthymine formed by ethylating and propylating agents were also efficiently reduced by either hAGT-03 or Ogt, whereas hAGT had little effect irrespective of NER status. These results show that specific alterations in the hAGT active site facilitate efficient recognition and repair of O(4)-alkylthymines and reveal damage-dependent interactions of base and nucleotide excision repair.
MeSH term(s)	Alkylation/physiology ; Catalytic Domain ; DNA Adducts/metabolism ; DNA Damage/physiology ; DNA Repair/physiology ; Escherichia coli/genetics ; Ethane/metabolism ; Humans ; Methane/metabolism ; Mutagenesis/physiology ; O(6)-Methylguanine-DNA Methyltransferase/chemistry ; O(6)-Methylguanine-DNA Methyltransferase/genetics ; O(6)-Methylguanine-DNA Methyltransferase/metabolism ; Propane/metabolism ; Protein Structure, Tertiary ; Thymine/metabolism
Chemical Substances	DNA Adducts ; O(6)-Methylguanine-DNA Methyltransferase (EC 2.1.1.63) ; Ethane (L99N5N533T) ; Methane (OP0UW79H66) ; Thymine (QR26YLT7LT) ; Propane (T75W9911L6)
Language	English
Publishing date	2009-12-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M109.045518
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Article: Repair of O⁴-Alkylthymine by O⁶-Alkylguanine-DNA Alkyltransferases

Fang, Qingming / Kanugula, Sreenivas / Tubbs, Julie L / Tainer, John A / Pegg, Anthony E

Journal of biological chemistry. 2010 Mar. 12, v. 285, no. 11

2010

Abstract: O⁶-Alkylguanine-DNA alkyltransferase (AGT) plays a major role in repair of the cytotoxic and mutagenic lesion O⁶-methylguanine (m⁶G) in DNA. Unlike the Escherichia coli alkyltransferase Ogt that also repairs O⁴-methylthymine (m⁴T) efficiently, the human ... ...

Abstract	O⁶-Alkylguanine-DNA alkyltransferase (AGT) plays a major role in repair of the cytotoxic and mutagenic lesion O⁶-methylguanine (m⁶G) in DNA. Unlike the Escherichia coli alkyltransferase Ogt that also repairs O⁴-methylthymine (m⁴T) efficiently, the human AGT (hAGT) acts poorly on m⁴T. Here we made several hAGT mutants in which residues near the cysteine acceptor site were replaced by corresponding residues from Ogt to investigate the basis for the inefficiency of hAGT in repair of m⁴T. Construct hAGT-03 (where hAGT sequence -V¹⁴⁹CSSGAVGN¹⁵⁷- was replaced with the corresponding Ogt -I¹⁴³GRNGTMTG¹⁵¹-) exhibited enhanced m⁴T repair activity in vitro compared with hAGT. Three AGT proteins (hAGT, hAGT-03, and Ogt) exhibited similar protection from killing by N-methyl-N'-nitro-N-nitrosoguanidine and caused a reduction in m⁶G-induced G:C to A:T mutations in both nucleotide excision repair (NER)-proficient and -deficient Escherichia coli strains that lack endogenous AGTs. hAGT-03 resembled Ogt in totally reducing the m⁴T-induced T:A to C:G mutations in NER-proficient and -deficient strains. Surprisingly, wild type hAGT expression caused a significant but incomplete decrease in NER-deficient strains but a slight increase in T:A to C:G mutation frequency in NER-proficient strains. The T:A to C:G mutations due to O⁴-alkylthymine formed by ethylating and propylating agents were also efficiently reduced by either hAGT-03 or Ogt, whereas hAGT had little effect irrespective of NER status. These results show that specific alterations in the hAGT active site facilitate efficient recognition and repair of O⁴-alkylthymines and reveal damage-dependent interactions of base and nucleotide excision repair.
Language	English
Dates of publication	2010-0312
Size	p. 8185-8195.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
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Article ; Online: An evaluation of acuity adjustment metrics to track medication expense over time.

Brink, Heidi L / Naseman, Ryan W / Porter, Kyle / Reed, Erica E / Tubbs, Crystal

American journal of health-system pharmacy : AJHP : official journal of the American Society of Health-System Pharmacists

2015 Volume 72, Issue 24, Page(s) 2157–2165

Abstract: ... conducted at the Ohio State University Wexner Medical Center. All inpatient discharges between July 1, 2012 ...

Abstract	Purpose: The acuity adjustment metric that correlates most closely with actual medication expense at a large, tertiary care academic medical center was investigated. Methods: This evaluation was conducted at the Ohio State University Wexner Medical Center. All inpatient discharges between July 1, 2012, and March 31, 2013, were included in this study. Patient medical and financial records were used to obtain the diagnosis-related group (DRG) codes and total medication cost for each patient discharge. The primary DRG for each patient was then used to assign the corresponding relative weight (RW) and pharmacy intensity weight (PIW). The correlation between actual and predicted medication expenditure was determined for every DRG for both RW and PIW. Since this compares cost at the DRG level, RW and PIW were used as markers for case-mix index (CMI) and pharmacy intensity score (PIS), respectively. Results: At this single institution, medication cost per discharge was more strongly correlated with PIW (as a marker for PIS) than with RW (as a marker for CMI). Extrapolating these data to hospital-specific values, the results suggest that PIS is more strongly correlated with overall medication expense than CMI and therefore a better adjustment metric for monitoring medication expense over time. Conclusion: A single-institution study demonstrated that PIW was more strongly correlated than RW with actual medication expenditure. PIS may be a more accurate acuity metric than CMI for predicting changes in drug expense over time.
MeSH term(s)	Drug Costs/trends ; Health Care Costs/trends ; Humans ; Patient Acuity ; Patient Discharge/economics ; Patient Discharge/trends ; Pharmacy Service, Hospital/economics ; Pharmacy Service, Hospital/trends ; Time Factors
Language	English
Publishing date	2015-11-19
Publishing country	England
Document type	Evaluation Studies ; Journal Article
ZDB-ID	1224627-x
ISSN	1535-2900 ; 1079-2082
ISSN (online)	1535-2900
ISSN	1079-2082
DOI	10.2146/ajhp140755
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Article ; Online: A research protocol for testing relationships between nurse workload, missed nursing care and neonatal outcomes: the neonatal nursing care quality study.

Tubbs-Cooley, Heather L / Pickler, Rita H / Mark, Barbara A / Carle, Adam C

Journal of advanced nursing

2015 Volume 71, Issue 3, Page(s) 632–641

Abstract: ... data extracted from the electronic health record. Funding for the study began in July 2012 ...

Abstract	Aim: We describe an innovative research protocol to test the role of missed nursing care as a mediator of the association between nurse workload and patient outcomes in the neonatal intensive care unit. Background: Increases in nurses' workloads are associated with adverse patient outcomes in neonatal intensive care settings. Missed nursing care is a frequently hypothesized explanation for the association between workload and outcomes. Few studies to date have tested missed care as a variable that mediates the workload-outcomes relationship. Design: We use a longitudinal, observational study design. Methods: We will recruit approximately 125 nurses (80% of target population) providing direct patient care in one neonatal intensive care unit. Four, 6-week data collection cycles occur over 1 year. At the end of every shift, nurses report on their workloads and the frequency with which specific patient care activities were missed for each infant cared for during the shift. Infant-specific nurse reports of missed care are linked to shift-level infant outcomes data extracted from the electronic health record. Funding for the study began in July 2012; Research Ethics Committee approval was granted in December 2012. Discussion: Missed care may explain the effects of nurse workload on patient outcomes. This research will generate preliminary evidence regarding the causal relationships among nurses' workloads, missed care and infant outcomes that we will confirm in a future multi-site study.
MeSH term(s)	Clinical Competence/standards ; Humans ; Infant, Newborn ; Intensive Care, Neonatal/standards ; Longitudinal Studies ; Neonatal Nursing/standards ; Patient Outcome Assessment ; Patient Safety ; Quality of Health Care/standards ; Workload
Language	English
Publishing date	2015-03
Publishing country	England
Document type	Journal Article ; Observational Study ; Research Support, Non-U.S. Gov't
ZDB-ID	197634-5
ISSN	1365-2648 ; 0309-2402
ISSN (online)	1365-2648
ISSN	0309-2402
DOI	10.1111/jan.12507
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Article ; Online: Alkyltransferase-like protein (Atl1) distinguishes alkylated guanines for DNA repair using cation-π interactions.

Wilkinson, Oliver J / Latypov, Vitaly / Tubbs, Julie L / Millington, Christopher L / Morita, Rihito / Blackburn, Hannah / Marriott, Andrew / McGown, Gail / Thorncroft, Mary / Watson, Amanda J / Connolly, Bernard A / Grasby, Jane A / Masui, Ryoji / Hunter, Christopher A / Tainer, John A / Margison, Geoffrey P / Williams, David M

Proceedings of the National Academy of Sciences of the United States of America

2012 Volume 109, Issue 46, Page(s) 18755–18760

Abstract: Alkyltransferase-like (ATL) proteins in Schizosaccharomyces pombe (Atl1) and Thermus thermophilus (TTHA1564) protect against the adverse effects of DNA alkylation damage by flagging O(6)-alkylguanine lesions for nucleotide excision repair (NER). We show ... ...

Abstract	Alkyltransferase-like (ATL) proteins in Schizosaccharomyces pombe (Atl1) and Thermus thermophilus (TTHA1564) protect against the adverse effects of DNA alkylation damage by flagging O(6)-alkylguanine lesions for nucleotide excision repair (NER). We show that both ATL proteins bind with high affinity to oligodeoxyribonucleotides containing O(6)-alkylguanines differing in size, polarity, and charge of the alkyl group. However, Atl1 shows a greater ability than TTHA1564 to distinguish between O(6)-alkylguanine and guanine and in an unprecedented mechanism uses Arg69 to probe the electrostatic potential surface of O(6)-alkylguanine, as determined using molecular mechanics calculations. An unexpected consequence of this feature is the recognition of 2,6-diaminopurine and 2-aminopurine, as confirmed in crystal structures of respective Atl1-DNA complexes. O(6)-Alkylguanine and guanine discrimination is diminished for Atl1 R69A and R69F mutants, and S. pombe R69A and R69F mutants are more sensitive toward alkylating agent toxicity, revealing the key role of Arg69 in identifying O(6)-alkylguanines critical for NER recognition.
MeSH term(s)	Alkyl and Aryl Transferases/chemistry ; Alkyl and Aryl Transferases/genetics ; Alkyl and Aryl Transferases/metabolism ; Alkylation ; Amino Acid Substitution ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Crystallography, X-Ray ; DNA Repair/physiology ; Guanine/chemistry ; Guanine/metabolism ; Mutation, Missense ; Oligodeoxyribonucleotides/chemistry ; Oligodeoxyribonucleotides/genetics ; Oligodeoxyribonucleotides/metabolism ; Protein Binding ; Protein Structure, Tertiary ; Schizosaccharomyces/enzymology ; Schizosaccharomyces/genetics ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; Thermus thermophilus/enzymology
Chemical Substances	Bacterial Proteins ; Oligodeoxyribonucleotides ; Schizosaccharomyces pombe Proteins ; Guanine (5Z93L87A1R) ; ATL1 protein, S pombe (EC 2.5.-) ; Alkyl and Aryl Transferases (EC 2.5.-)
Language	English
Publishing date	2012-10-29
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1209451109
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