Earlier, polyclonal antibodies to Escherichia coli RecA protein were used to identify immunologically related proteins in meiotic spermatocytes of different eukaryotes. At least one such protein proved to be a component of the synaptonemal complex (SC) [1]. Subsequent experiments on localization of RecA-like antigens in SCs of spermatocytes were performed by indirect immunocytochemical methods and electron microscopy, which showed that RecA-like protein(s) at early leptotene are largely associated with chromatin. During SC formation (at leptotene and zygotene), they are found in both lateral elements and the central space of SC. In some cases, RecA-like proteins are associated with SC substructures that resemble recombination nodules. When spermatocytes enter late diplotene, Rec-A-like proteins cease to be detected in SC structures.
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Nat Commun
November 2024
Institute of Medical Microbiology, University of Zurich, Zurich, Switzerland.
Mechanisms by which G-patch activators tune the processive multi-tasking ATP-dependent RNA helicase Prp43 (DHX15 in humans) to productively remodel diverse RNA:protein complexes remain elusive. Here, a comparative study between a herein and previously characterized activators, Tma23 and Pxr1, respectively, defines segments that organize Prp43 function during ribosome assembly. In addition to the activating G-patch, we discover an inhibitory segment within Tma23 and Pxr1, I-patch, that restrains Prp43 ATPase activity.
View Article and Find Full Text PDFNat Commun
October 2024
Kev Laboratory of Microbial Pathogenesis and Interventions of Fuian Province University, the Key Laboratory of inmate lmmune Biology of Fuijian Province, Biomedical Research Center of South China, Key Laboratory of Opto Electronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal University, Fuzhou, 350117, China.
Appl Biochem Biotechnol
December 2024
Dongguan Key Laboratory of Public Health Laboratory Science, School of Public Health, Guangdong Medical University, Dongguan, 523808, People's Republic of China.
Helicases, which utilize ATP hydrolysis to separate nucleic acid duplexes, play crucial roles in DNA and RNA replication, repair, recombination, and transcription. Categorized into the major groups superfamily 1 (SF1) and superfamily 2 (SF2), alongside four minor groups, these proteins exhibit a conserved catalytic core indicative of a shared evolutionary origin while displaying functional diversity through interactions with various substrates. This review summarizes the structures, functions and mechanisms of SF1 and SF2 helicases, with an emphasis on conserved ATPase sites and RecA-like domains essential for their enzymatic and nucleic acid binding capabilities.
View Article and Find Full Text PDFBiochemistry
January 2024
Department of Chemistry and Biochemistry, Utah State University, Logan, Utah 84322, United States.
Mtr4 is an essential RNA helicase involved in nuclear RNA processing and degradation and is a member of the Ski2-like helicase family. Ski2-like helicases share a common core architecture that includes two RecA-like domains, a winged helix, and a helical bundle (HB) domain. In Mtr4, a short C-terminal tail immediately follows the HB domain and is positioned at the interface of the RecA-like domains.
View Article and Find Full Text PDFNucleic Acids Res
November 2023
Department of Agricultural Biotechnology, Seoul National University, Seoul 08826, Korea.
Bacteriophages (phages) are viruses that infect bacteria and archaea. To fend off invading phages, the hosts have evolved a variety of anti-phage defense mechanisms. Gabija is one of the most abundant prokaryotic antiviral systems and consists of two proteins, GajA and GajB.
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