The PIP and TIP aquaporins in wheat form a large and diverse family with unique gene structures and functionally important features

被引:65
作者
Forrest, Kerrie L. [1 ]
Bhave, Mrinal [1 ]
机构
[1] Swinburne Univ Technol, Fac Life & Social Sci, Ctr Environm Biotechnol, Hawthorn, Vic 3122, Australia
关键词
major intrinsic proteins; aquaporins; wheat; abiotic stress;
D O I
10.1007/s10142-007-0065-4
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
Aquaporins, members of major intrinsic proteins (MIPs), transport water across cellular membranes and play vital roles in all organisms. Adversities such as drought, salinity, or chilling affect water uptake and transport, and numerous plant MIPs are reported to be differentially regulated under such stresses. However, MIP genes have been not yet been characterized in wheat, the largest cereal crop. We have identified 24 PIP and 11 TIP aquaporin genes from wheat by gene isolation and database searches. They vary extensively in lengths, numbers, and sequences of exons and introns, and sequences and cellular locations of predicted proteins, but the intron positions (if present) are characteristic. The putative PIP proteins show a high degree of conservation of signature sequences or residues for membrane integration, water transport, and regulation. The TIPs are more diverse, some with potential for water transport and others with various selectivity filters including a new combination. Most genes appear to be expressed as expressed sequence tags, while two are likely pseudogenes. Many of the genes are highly identical to rice but some are unique, and many correspond to genes that show differential expression under salinity and/or drought. The results provide extensive information for functional studies and developing markers for stress tolerance.
引用
收藏
页码:115 / 133
页数:19
相关论文
共 81 条
[1]   Aquaporin localization - how valid are the TIP and PIP labels? [J].
Barkla, BJ ;
Vera-Estrella, R ;
Pantoja, O ;
Kirch, HH ;
Bohnert, HJ .
TRENDS IN PLANT SCIENCE, 1999, 4 (03) :86-88
[2]   Drought and salt tolerance in plants [J].
Bartels, D ;
Sunkar, R .
CRITICAL REVIEWS IN PLANT SCIENCES, 2005, 24 (01) :23-58
[3]   Point mutations in the aromatic/arginine region in aquaporin 1 allow passage of urea, glycerol, ammonia, and protons [J].
Beitz, E ;
Wu, BH ;
Holm, LM ;
Schultz, JE ;
Zeuthen, T .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (02) :269-274
[4]   STRUCTURAL-ANALYSIS OF AT MIP FAMILY PROTEIN FROM THE DIGESTIVE-TRACT OF CICADELLA-VIRIDIS [J].
BEURON, F ;
LECAHEREC, F ;
GUILLAM, MT ;
CAVALIER, A ;
GARRET, A ;
TASSAN, JP ;
DELAMARCHE, C ;
SCHULTZ, P ;
MALLOUH, V ;
ROLLAND, JP ;
HUBERT, JF ;
GOURANTON, J ;
THOMAS, D .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (29) :17414-17422
[5]   The Nicotiana tabacum plasma membrane aquaporin NtAQP1 is mercury-insensitive and permeable for glycerol [J].
Biela, A ;
Grote, K ;
Otto, B ;
Hoth, S ;
Hedrich, R ;
Kaldenhoff, R .
PLANT JOURNAL, 1999, 18 (05) :565-570
[6]   The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain [J].
Brandizzi, F ;
Frangne, N ;
Marc-Martin, S ;
Hawes, C ;
Neuhaus, JM ;
Paris, N .
PLANT CELL, 2002, 14 (05) :1077-1092
[7]  
Carvajal M, 1996, PLANTA, V199, P372, DOI 10.1007/BF00195729
[8]   Regulation of plant aquaporin activity [J].
Chaumont, F ;
Moshelion, M ;
Daniels, MJ .
BIOLOGY OF THE CELL, 2005, 97 (10) :749-764
[9]   Plasma membrane intrinsic proteins from maize cluster in two sequence subgroups with differential aquaporin activity [J].
Chaumont, F ;
Barrieu, F ;
Jung, R ;
Chrispeels, MJ .
PLANT PHYSIOLOGY, 2000, 122 (04) :1025-1034
[10]   Aquaporins constitute a large and highly divergent protein family in maize [J].
Chaumont, F ;
Barrieu, F ;
Wojcik, E ;
Chrispeels, MJ ;
Jung, R .
PLANT PHYSIOLOGY, 2001, 125 (03) :1206-1215