title: Thermal-stable proteins of fruit of long-living Sacred LotusNelumbo nuciferaGaertn var. China Antique.
abstract: Single-seeded fruit of the sacred lotusNelumbo nuciferaGaertn var. China Antique from NE China have viability as long as ~1300 years determined by direct radiocarbon-dating, having a germination rate of 84%. The pericarp, a fruit tissue that encloses the single seeds ofNelumbo, is considered one of the major factors that contribute to fruit longevity. Proteins that are heat stable and have protective function may be equally important to seed viability. We show proteins ofNelumbofruit that are able to withstand heating, 31% of which remained soluble in the 110°C-treated embryo-axis of a 549-yr-old fruit and 76% retained fluidity in its cotyledons. Genome of Nelumbo is published. The amino-acid sequences of 11 "thermal proteins" (soluble at 100°C) of modernNelumboembryo-axes and cotyledons, identified by mass spectrometry, Western blot and bioassay, are assembled and aligned with those of an archaeal-hyperthermophileMethancaldococcus jannaschii(Mj; an anaerobic methanogen having a growth optimum of 85°C) and with five mesophile angiosperms. These thermal proteins have roles in protection and repair under stress. More than half of theNelumbothermal proteins (55%) are present in the archaean Mj, indicating their long-term durability and history. OneNelumboprotein-repair enzyme exhibits activity at 100°C, having a higher heat-tolerance than that of Arabidopsis. A list of 30 sequenced but unassembled thermal proteins ofNelumbois supplemented.
authors.affiliation: IGPP Center for the Study of Evolution and Origin of Life, Department of Ecology and Evolutionary Biology, University of California, Los Angeles, Geology Building, Room 5676, 595 Charles E. Young Drive East, Los Angeles, CA 90095-1567, USA, Telephone: (310) 825-2891, , shenmiller@lifesci.ucla.edu.
authors.forename: J
authors.initials: J
authors.lastname: Shen-Miller
authors.affiliation: Lehrstuhl Mikrobiologie Regensburg University Universitat Str. 31 93053 Regensburg, Germany.
authors.forename: Petra
authors.initials: P
authors.lastname: Lindner
authors.affiliation: Department of Chemistry and Biochemistry University of California, Los Angeles 402 Boyer Hall, Hilgard Avenue Los Angeles, CA 90095-1569, USA.
authors.forename: Yongming
authors.initials: Y
authors.lastname: Xie
authors.affiliation: Department of Chemistry and Biochemistry University of California, Los Angeles 640 Boyer Hall, Hilgard Avenue Los Angeles, CA 90095-1570, USA.
authors.forename: Sarah
authors.initials: S
authors.lastname: Villa
authors.affiliation: Department of Chemistry and Biochemistry University of California, Los Angeles 402 Boyer Hall, Hilgard Avenue Los Angeles, CA 90095-1569, USA.
authors.forename: Kerry
authors.initials: K
authors.lastname: Wooding
authors.affiliation: Department of Chemistry and Biochemistry University of California, Los Angeles 640 Boyer Hall, Hilgard Avenue Los Angeles, CA 90095-1570, USA.
authors.forename: Steven G
authors.initials: SG
authors.lastname: Clarke
authors.affiliation: Department of Chemistry and Biochemistry University of California, Los Angeles 402 Boyer Hall, Hilgard Avenue Los Angeles, CA 90095-1569, USA.
authors.forename: Rachel R O
authors.initials: RR
authors.lastname: Loo
authors.affiliation: Department of Chemistry and Biochemistry University of California, Los Angeles 402 Boyer Hall, Hilgard Avenue Los Angeles, CA 90095-1569, USA.
authors.forename: Joseph A
authors.initials: JA
authors.lastname: Loo
keywords: 30 Additional Thermal-Proteins; Eleven 100°C-Heat-Soluble Proteins; Hyperthermophile-Mesophile Protein-Alignments; Nelumbo nucifera China Antique; Stress-and-Repair Proteins