Cloning and Expression Pattern Analysis of Ectomycorrhizal Purple Acid Phosphatase Gene in Pinus massoniana Lamb.

ZHANG Ting; DING Gui-jie; WEN Xiao-peng

Volume 29 Issue 6

Article Contents

Turn off MathJax

Article Navigation > Forest Research > 2016 > 29(6): 797-806

Citation:

Cloning and Expression Pattern Analysis of Ectomycorrhizal Purple Acid Phosphatase Gene in Pinus massoniana Lamb.

1.
The Key Laboratory of Plant Resource Conservation and Germplasm Innovation in Mountainous Region (Ministry of Education), Institute of Agro-bioengineering and College of Life Sciences, Guizhou University, Guiyang 550025, Guizhou, China
2.
College of Forestry, Guizhou University, Guiyang 550025, Guizhou China

Received Date: 2015-12-14

Abstract

[Objective] To study the function of purple acid phosphatase gene and the response of phosphorus deficiency stress in Masson pine (Pinus massoniana). [Methods] The full-length sequence of PAP gene (PmPAP1) was cloned from this germplasm by RACE methodology, subsequently, multiple alignments of amino acid sequences, construction of phylogenetic tree, as well as the bioinformatics analysis were carried out. [Results] The results showed that PmPAP1 was obtained (GenBank accession number: KT390746), whose full-length cDNA sequence was 2,520 bp and the corresponding lengths of open reading frames (ORF) was 1,869 bp, which contained 622 amino acid residues, including a typical conserved domain and belonged to a high molecular weight protein. PmPAP1 had signal peptide and non-transmembrane domain, thus, it was presumably localized in matrix of cytoplasm or organelles, which demonstrated high homology with Nelumbo nucifera Gaertn. and Amborella trichopoda Baill., reflecting the considerably ancient and strict conservation during the evolutionary process. The temporal and spatial expression profiles showed that the expression level of PmPAP1 was induced by ectomycorrhizal symbiosis, which was expressed in different tissues of P. massoniana, the expression level of root was significantly higher than that of stem and leaf. The expression of PmPAP1 was correlated with the phosphorus status of soil in both non-and ectomycorrhizal plants, and its expression might be intensively up-regulated by low phosphorus stress; conversely, high phosphorus level inhibited its expression. Further, the activity of acid phosphatase continued to rise in roots under low phosphorous stress, indicating that the acid phosphatase was time-dependent on the low phosphorus supply. [Conclusion] A PmPAP1 was cloned and characterized for the first time from P. massoniana, especially its enhanced expression pattern by ectomycorrhizal symbiosis under low phosphorus stress, which provided new information about the role of ectomycorrhizal fungi.
- Pinus massoniana,
- ectomycorrhizal fungi,
- purple acid phosphatase gene,
- Expression pattern analysis

References

[1]	Klabunde T, Sträter N, Krebs B, et al. Structural relationship between the mammalian Fe (Ⅲ)-Fe (Ⅱ) and the Fe (Ⅲ)-Zn (Ⅱ) plant purple acid phosphatases[J]. Febs Letters, 1995, 367(1): 56-60.
[2]	Schenk G, Guddat L W, Ge Y, et al. Identification of mammalian-like purple acid phosphatases in a wide range of plants[J]. Gene, 2000, 250(1): 117-125.
[3]	Cashikar A G, Kumaresan R, Rao N M. Biochemical characterization and subcellular localization of the red kidney bean purple acid phosphatase[J]. Plant Physiology, 1997, 114(3): 907-915.
[4]	Oddie G W, Schenk G, Angel N Z, et al. Structure, function, and regulation of tartrate-resistant acid phosphatase[J]. Bone, 2000, 27(5): 575-584.
[5]	Yoneyama T, Taira M, Suzuki T, et al. Expression and characterization of a recombinant unique acid phosphatase from kidney bean hypocotyl exhibiting chloroperoxidase activity in the yeast pichia pastoris[J]. Protein expression and purification, 2007, 53(1): 31-39.
[6]	Carla E. Hegeman, Elizabeth A. Grabau. A novel phytase with sequence similarity to purple acid hosphatases is expressed in cotyledons of germinating soybean seedlings[J]. Plant Physiol, 2001, 126: 1598-1608.
[7]	Li C, Gui S, Yang T, et al. Identification of soybean purple acid phosphatase genes and their expression responses to phosphorus availability and symbiosis[J]. Annals of botany, 2012, 109(1): 275-285.
[8]	Kaida R, Hayashi T, Kaneko T S. Purple acid phosphatase in the walls of tobacco cells[J]. Phytochemistry, 2008, 69(14): 2546-2551.
[9]	Zimmermann P, Regierer B, Kossmann J, et al. Differential expression of three purple acid phosphatases from potato[J]. Plant Biology, 2004, 6(5): 519-528.
[10]	Bozzo G G, Raghothama K G, Plaxton W C. Structural and kinetic properties of a novel purple acid hosphatase from phosphate-starved tomato (Lycopersicon esculentum) cell cultures[J]. Biochem, 2004, 377: 419-428.
[11]	Liao H, Wong FL, Phang TH, et al. GmPAP3, a novel purple acid phosphatase-like gene in soybean induced by NaCl stress but not phosphorus deficiency[J]. Gene, 2003, 318: 103-111.
[12]	Zhu H, Qian W, Lu X, et al. Expression patterns of purple acid phosphatase genes in Arabidopsis organs and functional analysis of AtPAP23 predominantly transcribed in flower[J]. Plant molecular biology, 2005, 59(4): 581-594.
[13]	Kaida R, Sage-Ono K, Kamada H, et al. Isolation and characterization of four cell wall purple acid phosphatase genes from tobacco cells[J]. Biochim Biophys Acta, 2003, 1625: 134-140.
[14]	Kaida R, Satoh Y, Bulone V, et al. Activation of β-glucan synthases by wall-bound purple acid phosphatase in tobacco cells[J]. Plant physiology, 2009, 150(4): 1822-1830.
[15]	Kaida R, Serada S, Norioka N, et al. Potential role for purple acid phosphatase in the dephosphorylation of wall proteins in tobacco cells[J]. Plant physiology, 2010, 153(2): 603-610.
[16]	马琼, 黄建国, 蒋剑波. 接种外生菌根真菌对马尾松幼苗生长的影响[J]. 福建林业科技, 2005, 2(32): 85-88.
[17]	周志春, 谢钰容, 金国庆, 等. 马尾松种源对磷肥的遗传反应及根际土壤营养差异[J]. 林业科学, 2003, 39(6): 62-67.
[18]	Olczak M, Morawiecka B, Watorek W. Plant purple acid phosphatases-genes, structures and biological function[J]. Acta biochimica polonica, 2003, 50(4): 1245-1256.
[19]	Beck J L, McConachie L A, Summors A C, et al. Properties of a purple phosphatase from red kidney bean: a zinc-iron metalloenzyme[J]. Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, 1986, 869(1): 61-68.
[20]	Zhang Q, Wang C, Tian J, et al. Identification of rice purple acid phosphatases related to posphate starvation signalling[J]. Plant Biology, 2011, 13(1): 7-15.
[21]	汋慬瑡楢潵湮?潥映?瀬栠潓獴灲栦愣琲攲?猻瑴慥牲瘠慎琬椠潆湲…爣攲猴瀶漻湨獬敩獣?愠湒搬?爼潥潭琾?慴爠捡桬椼琯敥捭琾甮爠敍?楣湨?牮楩捳敭嬠?嵦??健氠愨湢琩?做桮礠猨楡漩氠???ば?????????????????扳牥?孢??嵥??牯楮欠????噴敡湬攠歳汴慲慵獣???慥湳獛??愮洠扊敯牵獲???愠獯潦渠??牬慥杣杵???攠浢?敯瑬?慧汹??攱洹???传瀲瀵漹爨琴甩渺椠琷椳攷猭?昴漸爮?楢浲瀾牛漲瘲楝渠杍?灲桴潺猠灐栬漠牙畵猠?甬猠敓?敫晫晩楮捫椠敒測挠礼?業渾?捴爠潡灬?瀯汥慭渾琮猠孋?嵮??乩散眠?偮桤礠瑳潰汥???は??????????ぬ???????戠牭?孴??嵴??慯牦爠楡猠潣湯?????卥楤朠湨慩汳楴湩杤?楮湥?瑩桮攠?慨牥戠畭獥捴畡汬慬牯?浨祯捳潰牨牡桴楡穳慥汳?獣祡浬扣楩潮獥極獲孩?崠???椠掻爠潰扲楯潴汥??㈠ばと??????????????扊牯?孲??嵬?坯慦渠杂?塯??坧慩湣条?夠??呥業慩湳?????攱洹?攷琬?愲氷??攳洴???伲瘱攲爹收砭瀲爱攳猰猲椮渼杢??瑛倲?偝ㄠ??敡湢桵慮湤捥攠獔?瀠桋潲獥灢桳潥爠畂献?敔晨晥椠捤楩敭湥捴祡?椠湣?獮潴祥扲攠慩湮嬠?嵵??偬汥愠湡瑣?偤栠祰獨楯潳汰???ちび???ㄠ??????????び??扮爠?孲??嵥??楳??????婯桤略???????楓異???????敂浥?敬瑩?愠汈??敤浥???偲畧爬瀠氱改?愷挬椠搸?瀺栠漱猷瀷栭愱琹愸献攼獢?漾晛′?敝洠??牨慥扮楫搠潇瀬猠楃獡?瑲桩慮汧楴慯湮愠??故洬???捭潩浬灴慯牮愠瑓椠癅攬?愼湥慭氾祥獴椠獡?愼港摥?搾椮映晃敲特敳湴瑡楬慬汩?牡整杩畯汮愠瑡楮潤渠?扲祥?灩桭潩獮灡桲慹琠敘?摲敡灹爠楤癩慦瑦楲潡湣孴?嵯???楡潴污???桲攠浡???ひば?????????????????????扲牯?嬠??嵥?奴愠湰????坯慛湊杝???兣???楃???塴???景晧敲捡瑰獨?潣晡?灓桥潣獴灩桯潮爠畄猺??敩癯敬汯?潩湣?瑬栠敃?慹捳瑴楡癬楬瑯祧?潡晰?慹挬椠搱?瀹根漬猠瀵栵愨琱愲猩攺?椲渰‵爱漭漲琰猵′漮昼?桲社扛爲椵摝?牗楡捳敡?慩渠摊?椠瑙獡?灡慭牵敲湡琠獔嬬?嵓???桡楮湯攠獔攬??潥畭爾湥慴氠?潬昼?剥業挾攮?卓捥楣敲湥捴敥獤???ど??????????????????扸牰?孥??嵥?匠畩?匠?婬???楥畲????坴畳?????敵浰?敮琠?慮氠??敳浰????砠灴牯攠獰獨楯潳湰?慯湲摵?猠敤煥畦敩湣捩敥?癣慹牛楊慝琮椠潐湬?慮湴愠污祮獤椠獓?潩晬?愠′氰漰眳?瀠栲漴猸瀨栱漭爲甩猺?爱攲猹瀭漱渳猶椮瘼敢?朾敛渲收?娠浖健?健??楡湡??慅椠穊攬嬠?嵡???潲汳攠捈甬氠慂牲?偧汧愠湊琬??牥敭放摥楴渠条??土づ????????????ど???????扲爠?孭??嵯?呩楮慧渠????坰慨湯杲????婳桥愠湥杦?兩???敮浣?攠瑩?愠汣??数洠???佮癴敳牛?敝砮瀠牎敥獷猠楐潨湹?潯晬?佧獩偳?倬ㄠ?愰?′愬?爱漹漵琨?愩猺猠漳挰椶愭琳攲搰?愼换楲搾?瀲样潝猠灗桡慮瑧愠獌攬??楩渠捚爬攠慑獩敡摮?敗砬琠爼慥捭放汥汴甠污慬爼?潥牭朾愮渠楔捨?瀠桁潲獡灢桩潤牯異獳?畳琠楰汵楲穰慬瑥椠潡湣?楤渠?牨楯捳数孨?嵴???漠畁牴湐慁汐?漰映??渠瑰敲来牤慯瑭楩癮敡?側汬慹渠瑡??楯潣汩潡杴祥???ど??????????????????? and plays an important role in plant tolerance to phosphate limitation[J]. Plant Physiol, 2011, 157: 1283-99.
[22]	Robinson WD, Park J, Tran HT, et al. The secreted purple acid phosphatase is ozymes AtPAP12 and tPAP26 play a pivotal role in extracellular phosphate-scavenging by Arabidopsis thaliana[J]. Exp Bot, 2012, 63(18): 6531-6542.
[23]	Liang C, Sun L, Yao Z, et al. Comparative analysis of PvPAP gene family and their functions in response to phosphorus deficiency in common bean[J]. Plos one, 2012, 7(5): e38106-e38106.
[24]	Dai X, Wang Y, Yang A, et al. OsMYB2P-1, an R2R3MYB transcription factor, is involved in the regu

Proportional views

通讯作者: 陈斌, bchen63@163.com

1.
沈阳化工大学材料科学与工程学院沈阳 110142

Get Citation

PDF

XML

Article views(3132) PDF downloads(683) Cited by()

Proportional views

Cloning and Expression Pattern Analysis of Ectomycorrhizal Purple Acid Phosphatase Gene in Pinus massoniana Lamb.

1. The Key Laboratory of Plant Resource Conservation and Germplasm Innovation in Mountainous Region (Ministry of Education), Institute of Agro-bioengineering and College of Life Sciences, Guizhou University, Guiyang 550025, Guizhou, China

2. College of Forestry, Guizhou University, Guiyang 550025, Guizhou China

Received Date: 2015-12-14

Abstract: [Objective] To study the function of purple acid phosphatase gene and the response of phosphorus deficiency stress in Masson pine (Pinus massoniana). [Methods] The full-length sequence of PAP gene (PmPAP1) was cloned from this germplasm by RACE methodology, subsequently, multiple alignments of amino acid sequences, construction of phylogenetic tree, as well as the bioinformatics analysis were carried out. [Results] The results showed that PmPAP1 was obtained (GenBank accession number: KT390746), whose full-length cDNA sequence was 2,520 bp and the corresponding lengths of open reading frames (ORF) was 1,869 bp, which contained 622 amino acid residues, including a typical conserved domain and belonged to a high molecular weight protein. PmPAP1 had signal peptide and non-transmembrane domain, thus, it was presumably localized in matrix of cytoplasm or organelles, which demonstrated high homology with Nelumbo nucifera Gaertn. and Amborella trichopoda Baill., reflecting the considerably ancient and strict conservation during the evolutionary process. The temporal and spatial expression profiles showed that the expression level of PmPAP1 was induced by ectomycorrhizal symbiosis, which was expressed in different tissues of P. massoniana, the expression level of root was significantly higher than that of stem and leaf. The expression of PmPAP1 was correlated with the phosphorus status of soil in both non-and ectomycorrhizal plants, and its expression might be intensively up-regulated by low phosphorus stress; conversely, high phosphorus level inhibited its expression. Further, the activity of acid phosphatase continued to rise in roots under low phosphorous stress, indicating that the acid phosphatase was time-dependent on the low phosphorus supply. [Conclusion] A PmPAP1 was cloned and characterized for the first time from P. massoniana, especially its enhanced expression pattern by ectomycorrhizal symbiosis under low phosphorus stress, which provided new information about the role of ectomycorrhizal fungi.

HTML

Reference (24)

[1]	Klabunde T, Sträter N, Krebs B, et al. Structural relationship between the mammalian Fe (Ⅲ)-Fe (Ⅱ) and the Fe (Ⅲ)-Zn (Ⅱ) plant purple acid phosphatases[J]. Febs Letters, 1995, 367(1): 56-60.
[2]	Schenk G, Guddat L W, Ge Y, et al. Identification of mammalian-like purple acid phosphatases in a wide range of plants[J]. Gene, 2000, 250(1): 117-125.
[3]	Cashikar A G, Kumaresan R, Rao N M. Biochemical characterization and subcellular localization of the red kidney bean purple acid phosphatase[J]. Plant Physiology, 1997, 114(3): 907-915.
[4]	Oddie G W, Schenk G, Angel N Z, et al. Structure, function, and regulation of tartrate-resistant acid phosphatase[J]. Bone, 2000, 27(5): 575-584.
[5]	Yoneyama T, Taira M, Suzuki T, et al. Expression and characterization of a recombinant unique acid phosphatase from kidney bean hypocotyl exhibiting chloroperoxidase activity in the yeast pichia pastoris[J]. Protein expression and purification, 2007, 53(1): 31-39.
[6]	Carla E. Hegeman, Elizabeth A. Grabau. A novel phytase with sequence similarity to purple acid hosphatases is expressed in cotyledons of germinating soybean seedlings[J]. Plant Physiol, 2001, 126: 1598-1608.
[7]	Li C, Gui S, Yang T, et al. Identification of soybean purple acid phosphatase genes and their expression responses to phosphorus availability and symbiosis[J]. Annals of botany, 2012, 109(1): 275-285.
[8]	Kaida R, Hayashi T, Kaneko T S. Purple acid phosphatase in the walls of tobacco cells[J]. Phytochemistry, 2008, 69(14): 2546-2551.
[9]	Zimmermann P, Regierer B, Kossmann J, et al. Differential expression of three purple acid phosphatases from potato[J]. Plant Biology, 2004, 6(5): 519-528.
[10]	Bozzo G G, Raghothama K G, Plaxton W C. Structural and kinetic properties of a novel purple acid hosphatase from phosphate-starved tomato (Lycopersicon esculentum) cell cultures[J]. Biochem, 2004, 377: 419-428.
[11]	Liao H, Wong FL, Phang TH, et al. GmPAP3, a novel purple acid phosphatase-like gene in soybean induced by NaCl stress but not phosphorus deficiency[J]. Gene, 2003, 318: 103-111.
[12]	Zhu H, Qian W, Lu X, et al. Expression patterns of purple acid phosphatase genes in Arabidopsis organs and functional analysis of AtPAP23 predominantly transcribed in flower[J]. Plant molecular biology, 2005, 59(4): 581-594.
[13]	Kaida R, Sage-Ono K, Kamada H, et al. Isolation and characterization of four cell wall purple acid phosphatase genes from tobacco cells[J]. Biochim Biophys Acta, 2003, 1625: 134-140.
[14]	Kaida R, Satoh Y, Bulone V, et al. Activation of β-glucan synthases by wall-bound purple acid phosphatase in tobacco cells[J]. Plant physiology, 2009, 150(4): 1822-1830.
[15]	Kaida R, Serada S, Norioka N, et al. Potential role for purple acid phosphatase in the dephosphorylation of wall proteins in tobacco cells[J]. Plant physiology, 2010, 153(2): 603-610.
[16]	马琼, 黄建国, 蒋剑波. 接种外生菌根真菌对马尾松幼苗生长的影响[J]. 福建林业科技, 2005, 2(32): 85-88.
[17]	周志春, 谢钰容, 金国庆, 等. 马尾松种源对磷肥的遗传反应及根际土壤营养差异[J]. 林业科学, 2003, 39(6): 62-67.
[18]	Olczak M, Morawiecka B, Watorek W. Plant purple acid phosphatases-genes, structures and biological function[J]. Acta biochimica polonica, 2003, 50(4): 1245-1256.
[19]	Beck J L, McConachie L A, Summors A C, et al. Properties of a purple phosphatase from red kidney bean: a zinc-iron metalloenzyme[J]. Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, 1986, 869(1): 61-68.
[20]	Zhang Q, Wang C, Tian J, et al. Identification of rice purple acid phosphatases related to posphate starvation signalling[J]. Plant Biology, 2011, 13(1): 7-15.
[21]	汋慬瑡楢潵湮?潥映?瀬栠潓獴灲栦愣琲攲?猻瑴慥牲瘠慎琬椠潆湲…爣攲猴瀶漻湨獬敩獣?愠湒搬?爼潥潭琾?慴爠捡桬椼琯敥捭琾甮爠敍?楣湨?牮楩捳敭嬠?嵦??健氠愨湢琩?做桮礠猨楡漩氠???ば?????????????????扳牥?孢??嵥??牯楮欠????噴敡湬攠歳汴慲慵獣???慥湳獛??愮洠扊敯牵獲???愠獯潦渠??牬慥杣杵???攠浢?敯瑬?慧汹??攱洹???传瀲瀵漹爨琴甩渺椠琷椳攷猭?昴漸爮?楢浲瀾牛漲瘲楝渠杍?灲桴潺猠灐栬漠牙畵猠?甬猠敓?敫晫晩楮捫椠敒測挠礼?業渾?捴爠潡灬?瀯汥慭渾琮猠孋?嵮??乩散眠?偮桤礠瑳潰汥???は??????????ぬ???????戠牭?孴??嵴??慯牦爠楡猠潣湯?????卥楤朠湨慩汳楴湩杤?楮湥?瑩桮攠?慨牥戠畭獥捴畡汬慬牯?浨祯捳潰牨牡桴楡穳慥汳?獣祡浬扣楩潮獥極獲孩?崠???椠掻爠潰扲楯潴汥??㈠ばと??????????????扊牯?孲??嵬?坯慦渠杂?塯??坧慩湣条?夠??呥業慩湳?????攱洹?攷琬?愲氷??攳洴???伲瘱攲爹收砭瀲爱攳猰猲椮渼杢??瑛倲?偝ㄠ??敡湢桵慮湤捥攠獔?瀠桋潲獥灢桳潥爠畂献?敔晨晥椠捤楩敭湥捴祡?椠湣?獮潴祥扲攠慩湮嬠?嵵??偬汥愠湡瑣?偤栠祰獨楯潳汰???ちび???ㄠ??????????び??扮爠?孲??嵥??楳??????婯桤略???????楓異???????敂浥?敬瑩?愠汈??敤浥???偲畧爬瀠氱改?愷挬椠搸?瀺栠漱猷瀷栭愱琹愸献攼獢?漾晛′?敝洠??牨慥扮楫搠潇瀬猠楃獡?瑲桩慮汧楴慯湮愠??故洬???捭潩浬灴慯牮愠瑓椠癅攬?愼湥慭氾祥獴椠獡?愼港摥?搾椮映晃敲特敳湴瑡楬慬汩?牡整杩畯汮愠瑡楮潤渠?扲祥?灩桭潩獮灡桲慹琠敘?摲敡灹爠楤癩慦瑦楲潡湣孴?嵯???楡潴污???桲攠浡???ひば?????????????????????扲牯?嬠??嵥?奴愠湰????坯慛湊杝???兣???楃???塴???景晧敲捡瑰獨?潣晡?灓桥潣獴灩桯潮爠畄猺??敩癯敬汯?潩湣?瑬栠敃?慹捳瑴楡癬楬瑯祧?潡晰?慹挬椠搱?瀹根漬猠瀵栵愨琱愲猩攺?椲渰‵爱漭漲琰猵′漮昼?桲社扛爲椵摝?牗楡捳敡?慩渠摊?椠瑙獡?灡慭牵敲湡琠獔嬬?嵓???桡楮湯攠獔攬??潥畭爾湥慴氠?潬昼?剥業挾攮?卓捥楣敲湥捴敥獤???ど??????????????????扸牰?孥??嵥?匠畩?匠?婬???楥畲????坴畳?????敵浰?敮琠?慮氠??敳浰????砠灴牯攠獰獨楯潳湰?慯湲摵?猠敤煥畦敩湣捩敥?癣慹牛楊慝琮椠潐湬?慮湴愠污祮獤椠獓?潩晬?愠′氰漰眳?瀠栲漴猸瀨栱漭爲甩猺?爱攲猹瀭漱渳猶椮瘼敢?朾敛渲收?娠浖健?健??楡湡??慅椠穊攬嬠?嵡???潲汳攠捈甬氠慂牲?偧汧愠湊琬??牥敭放摥楴渠条??土づ????????????ど???????扲爠?孭??嵯?呩楮慧渠????坰慨湯杲????婳桥愠湥杦?兩???敮浣?攠瑩?愠汣??数洠???佮癴敳牛?敝砮瀠牎敥獷猠楐潨湹?潯晬?佧獩偳?倬ㄠ?愰?′愬?爱漹漵琨?愩猺猠漳挰椶愭琳攲搰?愼换楲搾?瀲样潝猠灗桡慮瑧愠獌攬??楩渠捚爬攠慑獩敡摮?敗砬琠爼慥捭放汥汴甠污慬爼?潥牭朾愮渠楔捨?瀠桁潲獡灢桩潤牯異獳?畳琠楰汵楲穰慬瑥椠潡湣?楤渠?牨楯捳数孨?嵴???漠畁牴湐慁汐?漰映??渠瑰敲来牤慯瑭楩癮敡?側汬慹渠瑡??楯潣汩潡杴祥???ど??????????????????? and plays an important role in plant tolerance to phosphate limitation[J]. Plant Physiol, 2011, 157: 1283-99.
[22]	Robinson WD, Park J, Tran HT, et al. The secreted purple acid phosphatase is ozymes AtPAP12 and tPAP26 play a pivotal role in extracellular phosphate-scavenging by Arabidopsis thaliana[J]. Exp Bot, 2012, 63(18): 6531-6542.
[23]	Liang C, Sun L, Yao Z, et al. Comparative analysis of PvPAP gene family and their functions in response to phosphorus deficiency in common bean[J]. Plos one, 2012, 7(5): e38106-e38106.
[24]	Dai X, Wang Y, Yang A, et al. OsMYB2P-1, an R2R3MYB transcription factor, is involved in the regu

Cloning and Expression Pattern Analysis of Ectomycorrhizal Purple Acid Phosphatase Gene in Pinus massoniana Lamb.

Abstract

References

Proportional views

通讯作者: 陈斌, bchen63@163.com

Proportional views

Cloning and Expression Pattern Analysis of Ectomycorrhizal Purple Acid Phosphatase Gene in Pinus massoniana Lamb.

HTML

Catalog

Export File

Citation

Format

Content