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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/ASCHD_ZYMMA ASCHD_ZYMMA] Shows sequence-specific endoribonuclease activity towards single-stranded RNA (ssRNA), with a preference for the bond between pyrimidine and adenine nucleotides. May also have 5'-exonuclease activity.<ref>PMID:28951575</ref> | | [https://www.uniprot.org/uniprot/ASCHD_ZYMMA ASCHD_ZYMMA] Shows sequence-specific endoribonuclease activity towards single-stranded RNA (ssRNA), with a preference for the bond between pyrimidine and adenine nucleotides. May also have 5'-exonuclease activity.<ref>PMID:28951575</ref> |
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| == Publication Abstract from PubMed ==
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| Activating signal cointegrator-1 homology (ASCH) domains were initially reported in human as a part of the ASC-1 transcriptional regulator, a component of a putative RNA-interacting protein complex; their presence has now been confirmed in a wide range of organisms. Here, we have determined the trigonal and monoclinic crystal structures of an ASCH domain-containing protein from Zymomonas mobilis (ZmASCH), and analyzed the structural determinants of its nucleic acid processing activity. The protein has a central beta-barrel structure with several nearby alpha-helices. Positively charged surface patches form a cleft that runs through the pocket formed between the beta-barrel and the surrounding alpha-helices. We further demonstrate by means of in vitro assays that ZmASCH binds nucleic acids, and degrades single-stranded RNAs in a magnesium ion-dependent manner with a cleavage preference for the phosphodiester bond between the pyrimidine and adenine nucleotides. ZmASCH also removes a nucleotide at the 5'-end. Mutagenesis studies, guided by molecular dynamics simulations, confirmed that three residues (Tyr47, Lys53, and Ser128) situated in the cleft contribute to nucleic acid-binding and RNA cleavage activities. These structural and biochemical studies imply that prokaryotic ASCH may function to control the cellular RNA amount.
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| Crystal structure of an ASCH protein from Zymomonas mobilis and its ribonuclease activity specific for single-stranded RNA.,Kim BN, Shin M, Ha SC, Park SY, Seo PW, Hofmann A, Kim JS Sci Rep. 2017 Sep 26;7(1):12303. doi: 10.1038/s41598-017-12186-w. PMID:28951575<ref>PMID:28951575</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| == References == | | == References == |
| <references/> | | <references/> |
