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      Phylogenetic analysis of mammalian SIP30 sequences indicating accelerated adaptation of functional domain in primates

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          Abstract

          SIP30, characterized by a coiled-coil functional domain, plays a key role in regulating synaptic vesicle exocytosis and is implicated in neuropathic pain resulting from peripheral nerve injury. Because neuropathic pain is studied in primates (including human), domesticated animals, and rodents, we conducted a phylogenetic analysis of SIP30 in selected species of these three groups of mammals. SIP30 exhibits a high degree of sequence divergence in comparison to its protein binding partners SNAP25 and ZW10, which show broad sequence conservation. Notably, we observed an increased rate of change in the highly conserved coiled-coil domain in the SIP30 protein, specifically within primates. This observation suggests an accelerated adaptation of this functional domain in primate species.

          Highlights

          • SIP30 plays a pivotal role in regulating synaptic vesicle exocytosis and neuropathic pain.

          • SIP30 exhibits greater sequence divergence compared to its binding partners.

          • The coiled-coil domain shows an elevated rate of change only within primates, and not in domesticated animals or rodents.

          • This suggests an accelerated adaptation of this functional domain in primates.

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          Most cited references35

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          MrBayes 3: Bayesian phylogenetic inference under mixed models.

          MrBayes 3 performs Bayesian phylogenetic analysis combining information from different data partitions or subsets evolving under different stochastic evolutionary models. This allows the user to analyze heterogeneous data sets consisting of different data types-e.g. morphological, nucleotide, and protein-and to explore a wide variety of structured models mixing partition-unique and shared parameters. The program employs MPI to parallelize Metropolis coupling on Macintosh or UNIX clusters.
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            Membrane fusion: grappling with SNARE and SM proteins.

            The two universally required components of the intracellular membrane fusion machinery, SNARE and SM (Sec1/Munc18-like) proteins, play complementary roles in fusion. Vesicular and target membrane-localized SNARE proteins zipper up into an alpha-helical bundle that pulls the two membranes tightly together to exert the force required for fusion. SM proteins, shaped like clasps, bind to trans-SNARE complexes to direct their fusogenic action. Individual fusion reactions are executed by distinct combinations of SNARE and SM proteins to ensure specificity, and are controlled by regulators that embed the SM-SNARE fusion machinery into a physiological context. This regulation is spectacularly apparent in the exquisite speed and precision of synaptic exocytosis, where synaptotagmin (the calcium-ion sensor for fusion) cooperates with complexin (the clamp activator) to control the precisely timed release of neurotransmitters that initiates synaptic transmission and underlies brain function.
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              Dating of the human-ape splitting by a molecular clock of mitochondrial DNA

              A new statistical method for estimating divergence dates of species from DNA sequence data by a molecular clock approach is developed. This method takes into account effectively the information contained in a set of DNA sequence data. The molecular clock of mitochondrial DNA (mtDNA) was calibrated by setting the date of divergence between primates and ungulates at the Cretaceous-Tertiary boundary (65 million years ago), when the extinction of dinosaurs occurred. A generalized least-squares method was applied in fitting a model to mtDNA sequence data, and the clock gave dates of 92.3 +/- 11.7, 13.3 +/- 1.5, 10.9 +/- 1.2, 3.7 +/- 0.6, and 2.7 +/- 0.6 million years ago (where the second of each pair of numbers is the standard deviation) for the separation of mouse, gibbon, orangutan, gorilla, and chimpanzee, respectively, from the line leading to humans. Although there is some uncertainty in the clock, this dating may pose a problem for the widely believed hypothesis that the pipedal creature Australopithecus afarensis, which lived some 3.7 million years ago at Laetoli in Tanzania and at Hadar in Ethiopia, was ancestral to man and evolved after the human-ape splitting. Another likelier possibility is that mtDNA was transferred through hybridization between a proto-human and a proto-chimpanzee after the former had developed bipedalism.
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                Author and article information

                Contributors
                Journal
                Biochem Biophys Rep
                Biochem Biophys Rep
                Biochemistry and Biophysics Reports
                Elsevier
                2405-5808
                01 January 2024
                March 2024
                01 January 2024
                : 37
                : 101631
                Affiliations
                [a ]Department of Genetics, Rutgers University, Piscataway, NJ, 08854, USA
                [b ]School of Biomedical Sciences, and Department of Biological Sciences, Kent State University, Kent, Ohio, 44242, USA
                [c ]Center of Alcohol & Substance Use Studies, Rutgers University, Piscataway, NJ, 08854, USA
                Author notes
                []Corresponding author. Department of Genetics, and Center of Alcohol & Substance Use Studies, Rutgers University, Piscataway, NJ, 08854, USA. yu@ 123456biology.rutgers.edu
                Article
                S2405-5808(23)00212-1 101631
                10.1016/j.bbrep.2023.101631
                10771893
                38188366
                6231e072-e86a-4490-b589-67b56f834d06
                © 2023 The Authors

                This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

                History
                : 17 November 2023
                : 21 December 2023
                : 27 December 2023
                Categories
                Short Communication

                sip30,coiled-coil domain,mammal gene,neuropathic pain
                sip30, coiled-coil domain, mammal gene, neuropathic pain

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