{"doi":"10.1042/bj20040153","title":"Identification of the first archaeal Type 1 RNase H gene from <i>Halobacterium</i> sp. NRC-1: archaeal RNase HI can cleave an RNA–DNA junction","abstract":"<jats:p>All the archaeal genomes sequenced to date contain a single Type 2 RNase H gene. We found that the genome of a halophilic archaeon, Halobacterium sp. NRC-1, contains an open reading frame with similarity to Type 1 RNase H. The protein encoded by the Vng0255c gene, possessed amino acid sequence identities of 33% with Escherichia coli RNase HI and 34% with a Bacillus subtilis RNase HI homologue. The B. subtilis RNase HI homologue, however, lacks amino acid sequences corresponding to a basic protrusion region of the E. coli RNase HI, and the Vng0255c has the similar deletion. As this deletion apparently conferred a complete loss of RNase H activity on the B. subtilis RNase HI homologue protein, the Vng0255c product was expected to exhibit no RNase H activity. However, the purified recombinant Vng0255c protein specifically cleaved an RNA strand of the RNA/DNA hybrid in vitro, and when the Vng0255c gene was expressed in an E. coli strain MIC2067 it could suppress the temperature-sensitive growth defect associated with the loss of RNase H enzymes of this strain. These results in vitro and in vivo strongly indicate that the Halobacterium Vng0255c is the first archaeal Type 1 RNase H. This enzyme, unlike other Type 1 RNases H, was able to cleave an Okazaki fragment-like substrate at the junction between the 3′-side of ribonucleotide and 5′-side of deoxyribonucleotide. It is likely that the archaeal Type 1 RNase H plays a role in the removal of the last ribonucleotide of the RNA primer from the Okazaki fragment during DNA replication.</jats:p>","journal":"Biochemical Journal","year":2004,"id":42195,"datarank":1.7352711963762897,"base_score":3.713572066704308,"endowment":3.713572066704308,"self_citation_contribution":0.5570358100056463,"citation_network_contribution":1.1782353863706434,"self_endowment_contribution":0.5570358100056463,"citer_contribution":1.1782353863706434,"corpus_percentile":null,"corpus_rank":null,"citation_count":40,"citer_count":35,"citers_with_citation_signal":32,"citers_with_endowment":32,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":202289,"name":"Hiroshi YANAGAWA","orcid":null,"position":1,"is_corresponding":false},{"id":202290,"name":"Masaru TOMITA","orcid":null,"position":2,"is_corresponding":false},{"id":202291,"name":"Mitsuhiro ITAYA","orcid":null,"position":3,"is_corresponding":false},{"id":202288,"name":"Naoto OHTANI","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":3.713572066704308,"endowment":3.713572066704308,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"15115438","pmcid":"PMC1133889","openalex_id":"https://openalex.org/W2089028383","authors":[],"funders":[],"total_grants":0,"fwci":2.8521,"citation_percentile":0.89560241,"influential_citations":4,"citation_trend":[{"year":2012,"count":4},{"year":2013,"count":2},{"year":2014,"count":4},{"year":2015,"count":2},{"year":2016,"count":1},{"year":2017,"count":2},{"year":2019,"count":4},{"year":2020,"count":2},{"year":2021,"count":1},{"year":2022,"count":1}],"oa_status":"bronze","license":null,"oa_locations":[{"url":"https://portlandpress.com/biochemj/article-pdf/381/3/795/719091/bj3810795.pdf","host_type":"journal"},{"url":"https://europepmc.org/articles/pmc1133889?pdf=render","host_type":"GREEN"},{"url":"https://portlandpress.com/biochemj/article-pdf/381/3/795/719091/bj3810795.pdf","host_type":"publisher"},{"url":"https://doi.org/10.1042/bj20040153","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/15115438","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/1133889","host_type":"repository"}],"fields_of_study":["Bacteriophages and microbial interactions","Bacterial Genetics and Biotechnology","RNA and protein synthesis mechanisms","Medicine","Biology","Amino Acid Sequence","Bacillus subtilis","Bacterial Proteins","Cations, Divalent","Cloning, Molecular","DNA","Escherichia coli","Evolution, Molecular","Genetic Complementation Test","Genome, Archaeal","Halobacterium","Molecular Sequence Data","Nucleic Acid Heteroduplexes","RNA","Ribonuclease H","Sequence Homology, Amino Acid","Substrate Specificity"],"mesh_terms":["Amino Acid Sequence","Bacillus subtilis","Bacterial Proteins","Cations, Divalent","Cloning, Molecular","DNA","Escherichia coli","Genetic Complementation Test","Halobacterium","Molecular Sequence Data","Nucleic Acid Heteroduplexes","RNA","Substrate Specificity","Ribonuclease H","Sequence Homology, Amino Acid","Evolution, Molecular","Genome, Archaeal"],"keywords":["RNase MRP","RNase PH","Biology","RNase P","RNase H","Ribonuclease III","RNA","Molecular biology","Ribonucleotide","Gene","Biochemistry","Nucleotide","RNA interference"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life in Land"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-13T23:39:55.850272Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}