The maize ALDH protein superfamily: linking structural features to functional specificities

被引:61
|
作者
Jimenez-Lopez, Jose C. [3 ,5 ]
Gachomo, Emma W. [2 ]
Seufferheld, Manfredo J. [4 ]
Kotchoni, Simeon O. [1 ]
机构
[1] Purdue Univ, Dept Agron, W Lafayette, IN 47907 USA
[2] Purdue Univ, Dept Bot & Plant Pathol, W Lafayette, IN 47907 USA
[3] Purdue Univ, Dept Biol Sci, W Lafayette, IN 47907 USA
[4] Univ Illinois UC, Dept Crop Sci, Urbana, IL USA
[5] CSIC, Dept Biochem Cell & Mol Biol Plants, EEZ, E-18008 Granada, Spain
关键词
MITOCHONDRIAL ALDEHYDE DEHYDROGENASE; GENE SUPERFAMILY; MOLECULAR-BASIS; MALE-STERILITY; MALE-FERTILITY; CYTOPLASM; TOXIN; EVOLUTIONARY; EXPRESSION; RESOURCES;
D O I
10.1186/1472-6807-10-43
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Background: The completion of maize genome sequencing has resulted in the identification of a large number of uncharacterized genes. Gene annotation and functional characterization of gene products are important to uncover novel protein functionality. Results: In this paper, we identify, and annotate members of all the maize aldehyde dehydrogenase (ALDH) gene superfamily according to the revised nomenclature criteria developed by ALDH Gene Nomenclature Committee (AGNC). The maize genome contains 24 unique ALDH sequences encoding members of ten ALDH protein families including the previously identified male fertility restoration RF2A gene, which encodes a member of mitochondrial class 2 ALDHs. Using computational modeling analysis we report here the identification, the physico-chemical properties, and the amino acid residue analysis of a novel tunnel like cavity exclusively found in the maize sterility restorer protein, RF2A/ALDH2B2 by which this protein is suggested to bind variably long chain molecular ligands and/or potentially harmful molecules. Conclusions: Our finding indicates that maize ALDH superfamily is the most expanded of plant ALDHs ever characterized, and the mitochondrial maize RF2A/ALDH2B2 is the only plant ALDH that harbors a newly defined pocket/cavity with suggested functional specificity.
引用
收藏
页数:14
相关论文
共 50 条
  • [21] STRUCTURAL FEATURES OF A SUPERFAMILY OF ZINC-ENDOPEPTIDASES - THE METZINCINS
    STOCKER, W
    BODE, W
    CURRENT OPINION IN STRUCTURAL BIOLOGY, 1995, 5 (03) : 383 - 390
  • [22] Identifying and manipulating structural determinates linking catalytic specificities in terpene synthases
    Greenhagen, Bryan T.
    O'Maille, Paul E.
    Noel, Joseph P.
    Chappell, Joe
    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (26) : 9826 - 9831
  • [23] SPECIFICITIES OF PROTEIN STRUCTURAL STATE IN ERYTHROCYTIC MEMBRANES
    CHERNITSKII, EA
    KONEV, SV
    KOZLOVA, NM
    LYSKOVA, TI
    LIN, EI
    DOKLADY AKADEMII NAUK SSSR, 1972, 207 (01): : 211 - +
  • [24] Functional and Structural Features of Disease-Related Protein Variants
    Savojardo, Castrense
    Babbi, Giulia
    Martelli, Pier Luigi
    Casadio, Rita
    INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2019, 20 (07):
  • [25] STRUCTURAL AND FUNCTIONAL FEATURES OF PROTEIN HANDLING IN THE KIDNEY PROXIMAL TUBULE
    CHRISTENSEN, EI
    NIELSEN, S
    SEMINARS IN NEPHROLOGY, 1991, 11 (04) : 414 - 439
  • [26] A STRUCTURAL SIGNATURE CHARACTERISTIC OF THE CALYCIN PROTEIN SUPERFAMILY
    FLOWER, DR
    PROTEIN AND PEPTIDE LETTERS, 1995, 2 (02): : 341 - 346
  • [27] Structural characterization of plant defensin protein superfamily
    Gachomo, Emma W.
    Jimenez-Lopez, Jose C.
    Kayode, Adechola Pierre Polycarpe
    Baba-Moussa, Lamine
    Kotchoni, Simeon O.
    MOLECULAR BIOLOGY REPORTS, 2012, 39 (04) : 4461 - 4469
  • [28] STRUCTURAL RELATIONSHIP OF STREPTAVIDIN TO THE CALYCIN PROTEIN SUPERFAMILY
    FLOWER, DR
    FEBS LETTERS, 1993, 333 (1-2) : 99 - 102
  • [29] Structural characterization of plant defensin protein superfamily
    Emma W. Gachomo
    Jose C. Jimenez-Lopez
    Adéchola Pierre Polycarpe Kayodé
    Lamine Baba-Moussa
    Simeon O. Kotchoni
    Molecular Biology Reports, 2012, 39 : 4461 - 4469
  • [30] Linking protein structural and functional change to mutation using amino acid networks
    Sotomayor-Vivas, Cristina
    Hernandez-Lemus, Enrique
    Dorantes-Gilardi, Rodrigo
    PLOS ONE, 2022, 17 (01):