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          Institute: MPI für evolutionäre Anthropologie     Collection: Publications MPI for Evolutionary Anthropology     Display Documents



  history
ID: 251571.0, MPI für evolutionäre Anthropologie / Publications MPI for Evolutionary Anthropology
Osteocalcin protein sequences of Neanderthals and modern primates
Authors:Nielsen-Marsh, Christina M.; Richards, Michael P.; Hauschka, Peter V.; Thomas-Oates, Jane E.; Trinkaus, Erik; Pettitt, Paul B.; Karavanic, Ivor; Poinar, Hendrik N.; Collins, Matthew J.
Language:English
Date of Publication (YYYY-MM-DD):2005-03-22
Title of Journal:Proceedings of the National Academy of Sciences of the United States of America
Volume:102
Issue / Number:12
Start Page:4409
End Page:4413
Review Status:not specified
Audience:Not Specified
Abstract / Description: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.
Free Keywords:[01500] Evolution
; Physiology and biochemistry
; Biochemistry and Molecular Biophysics; Paleobiology;
; Evolution and Adaptation
; [86215] Hominidae
; [86215] Hominidae, Primates, Mammalia, Vertebrata, Chordata,
; Animalia
; Hominidae: Animals, Chordates, Humans, Mammals, Primates,
; Vertebrate; Pongidae: Animals, Chordates, Mammals, Nonhuman
; Mammals, Nonhuman Vertebrates, Nonhuman Primates, Primates,
; Vertebrate
; Homo sapiens: species, human, common [Hominidae]; Homo
; neanderthalensis: species, neanderthal, common, Fossil [Hominidae];
; Pan troglodytes: species, chimpanzee, common [Pongidae]; Pongo
; pygmaeus: species, orangutan, common [Pongidae]; Gorilla gorilla
; gorilla: subspecies, gorilla, common [Pongidae]
; bone: skeletal system
; iron(II) ion: 15438-31-0; vitamin C: 50-81-7; molecular
; oxygen: 7782-44-7; osteocalcin; hydroxyproline: 6912-67-0;
; 2-oxoglutarate: 328-50-7; prolyl-4-hydroxylase: 9028-06-2;
; proline: 609-36-9, hydroxylation
; omnivorous dietary adaptation; biomolecular preservation
External Publication Status:published
Document Type:Article
Communicated by:Gisela Lausberg
Affiliations:MPI für evolutionäre Anthropologie/Department of Human Evolution
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