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Osteocalcin protein sequences of Neanderthals and modern primates

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons72878

Nielsen-Marsh,  Christina M.
Department of Human Evolution, Max Planck Institute for Evolutionary Anthropology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons72929

Richards,  Michael P.
Department of Human Evolution, Max Planck Institute for Evolutionary Anthropology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons72906

Poinar,  Hendrik N.
Department of Evolutionary Genetics, Max Planck Institute for Evolutionary Anthropology, Max Planck Society;

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Zitation

Nielsen-Marsh, C. M., Richards, M. P., Hauschka, P. V., Thomas-Oates, J. E., Trinkaus, E., Pettitt, P. B., et al. (2005). Osteocalcin protein sequences of Neanderthals and modern primates. Proceedings of the National Academy of Sciences of the United States of America, 102(12), 4409-4413.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-02D8-F
Zusammenfassung
We report here protein sequences of fossil hominids, from two Neanderthals dating to approximate to 75,000 years old from Shanidar Cave in Iraq. These sequences, the oldest reported fossil primate protein sequences, are of bone osteocalcin, which was extracted and sequenced by using MALDI-TOF/TOF mass spectrometry. Through a combination of direct sequencing and peptide mass mapping, we determined that Neanderthals have an osteocalcin amino acid sequence that is identical to that of modern humans. We also report complete osteocalcin sequences for chimpanzee (Pan troglodytes) and gorilla (Gorilla gorilla gorilla) and a partial sequence for orangutan (Pongo pygmaeus), all of which are previously unreported. We found that the osteocalcin sequences of Neanderthals, modern human, chimpanzee, and orangutan are unusual among mammals in that the ninth amino acid is proline (Pro-9), whereas most species have hydroxyproline (Hyp-9). Posttranslational hydroxylation of Pro-9 in osteocalcin by prolyl-4-hydroxylase requires adequate concentrations of vitamin C (L-ascorbic acid), molecular O-2, Fe2+, and 2-oxoglutarate, and also depends on enzyme recognition of the target proline substrate consensus sequence Leu-Gly-Ala-Pro-9-Ala-Pro-Tyr occurring in most mammals. in five species with Pro-9-Val-10, hydroxylation is blocked, whereas in gorilla there is a mixture of Pro-9 and Hyp-9. We suggest that the absence of hydroxylation of Pro-9 in Pan, Pongo, and Homo may reflect response to a selective pressure related to a decline in vitamin C in the diet during omnivorous dietary adaptation, either independently or through the common ancestor of these species.