Evolution of the EF-Hand Family of Proteins

Nakayama, Seiko; Kretsinger, Robert H.

doi:10.1146/annurev.bb.23.060194.002353

Cited by 192 publications

(127 citation statements)

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“…Interestingly there is a Ca 2ϩ -binding motif of the EF-hand loop type in the third small exon (49 bp) of these A. thaliana homologues, flanked by α-helical conformations ( Figure 1a). The sequence of 13 amino acids (positions D-266/V-278 in AtrbohD) matches the consensus sequence for the Ca 2ϩ -binding fold of the EF-hand (Nakayama and Kretsinger, 1994), with the only exception of L-187 in AtrbohB. The presence of the highly conserved motif in all the Atrboh proteins suggests a possible direct effect of Ca 2ϩ in the function of the NADPH oxidase in plants.…”

Section: Resultsmentioning

confidence: 60%

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Six Arabidopsis thaliana homologues of the human respiratory burst oxidase (gp91^phox)

et al. 1998

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SummaryAn NADPH oxidase analogous to that in mammalian phagocytes has been hypothesized to produce reactive oxygen species (ROS) in the plant defence response. A. thaliana contains at least six gp91 phox homologues, designated AtrbohA-F (A. thaliana Respiratory Burst Oxidase Homologues), which map to different positions. Transcripts of three of these genes can be detected in healthy plants by RNA gel blot analyses. The Atrboh gene products are closely related to gp91 phox and the intron locations suggest a common evolutionary origin. A putative EF-hand Ca 2⍣ -binding motif in the extended N-terminal region of the Atrboh proteins suggests a direct regulatory effect of Ca 2⍣ on the activity of the NADPH oxidase in plants.

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Section: Resultsmentioning

confidence: 60%

“…The box highlights the putative EF-hand. Beneath this box is the sequence of a canonical EF-hand (Nakayama and Kretsinger, 1994) where n is a hydrophobic residue, -is any residue and x, y and z contain oxygen within their side-chain. (b) C-terminus comparison of AtrbohA-F, OsrbohA, gp91 phox and FRE1 proteins.…”

Section: Discussionmentioning

confidence: 99%

Six Arabidopsis thaliana homologues of the human respiratory burst oxidase (gp91^phox)

et al. 1998

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“…By binding calcium, these proteins undergo conformational changes that enable interaction with and modulation of effector proteins that cause the physiological changes linked to the calcium stimulus. Many of these calcium-signal proteins are well characterized and have been subgrouped based on structural and biochemical features (Heizman and Hunziker, 1991;Nakayama and Kretsinger, 1994;Niki et al, 1996). The majority are intracellular constituents, but some members may be secreted and have intercellular actions (Zimmer et al, 1995).…”

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confidence: 99%

Characterization and Immunolocalization of a Cytosolic Calcium-Binding Protein from Brassica napus and Arabidopsis Pollen1

Rozwadowski

Zhao

Jackman³

et al. 1999

Plant Physiology

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Two low-molecular-weight proteins have been purified from Brassica napus pollen and a gene corresponding to one of them has been isolated. The gene encodes an 8.6-kD protein with two EFhand calcium-binding motifs and is a member of a small gene family in B. napus. The protein is part of a family of pollen allergens recently identified in several evolutionarily distant dicot and monocot plants. Homologs have been detected in Arabidopsis, from which one gene has been cloned in this study, and in snapdragon (Antirrhinum majus), but not in tobacco (Nicotiana tabacum). Expression of the gene in B. napus was limited to male tissues and occurred during the pollen-maturation phase of anther development. Both the B. napus and Arabidopsis proteins interact with calcium, and the potential for a calcium-dependent conformational change was demonstrated. Given this affinity for calcium, the cloned genes were termed BPC1 and APC1 (B. napus and Arabidopsis pollen calcium-binding protein 1, respectively). Immunolocalization studies demonstrated that BPC1 is found in the cytosol of mature pollen. However, upon pollen hydration and germination, there is some apparent leakage of the protein to the pollen wall. BPC1 is also concentrated on or near the surface of the elongating pollen tube. The essential nature of calcium in pollen physiology, combined with the properties of BPC1 and its high evolutionary conservation suggests that this protein plays an important role in pollination by functioning as a calcium-sensitive signal molecule.

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“…Ca 2C sensors are characterized by the presence in their sequence of the canonical Ca 2C -binding motif called EF-hand. 6 The Arabidopsis genome encodes at least 250 EF-hand proteins, which is much higher than in mammals, arguing for higher importance of this class of proteins in plants. 7 These Ca 2C sensors are classified into 4 major groups, the calcineurin-B like, the calciumdependent kinases, the calmodulin group and a closely related group, the CalModulin-Like protein (CML) family, which is specific to plants.…”

Section: Introductionmentioning

confidence: 99%

Respective contribution of CML8 and CML9, two arabidopsis calmodulin-like proteins, to plant stress responses

Zhu

Perez

Aldon

et al. 2017

Plant Signaling & Behavior

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In their natural environment, plants have to continuously face constraints such as biotic and abiotic stresses. To achieve their life cycle, plants have to perceive and interpret the nature, but also the strength of environmental stimuli to activate appropriate physiological responses. Nowadays, it is well established that signaling pathways are crucial steps in the implementation of rapid and efficient plant responses such as genetic reprogramming. It is also reported that rapid raises in calcium (Ca 2C ) levels within plant cells participate in these early signaling steps and are essential to coordinate adaptive responses. However, to be informative, calcium increases need to be decoded and relayed by calcium-binding proteins also referred as calcium sensors to carry-out the appropriate responses. In a recent study, we showed that CML8, an Arabidopsis calcium sensor belonging to the calmodulin-like (CML) protein family, promotes plant immunity against the phytopathogenic bacteria Pseudomonas syringae pv tomato (strain DC3000). Interestingly, other CML proteins such as CML9 were also reported to contribute to plant immunity using the same pathosystem. In this addendum, we propose to discuss about the specific contribution of these 2 CMLs in stress responses. KEYWORDSArabidopsis thaliana; biotic and abiotic stress responses; calmodulin-like protein; calcium sensor; pseudomonas syringaeIt is now well documented that most of external biotic and abiotic stimuli induce a rapid increase in free calcium levels within plant cells. 1 Calcium is considered as an ubiquitous and versatile second messenger. Indeed, calcium variations are at the heart of sophisticated signaling networks, integrating information from a diverse range of developmental cues and environmental challenges that ultimately will impact gene expression and cell physiology. 2 Interestingly, these variations can harbour stimulusspecific properties 3 and according to the nature and strength of the stimuli, calcium variations display differences in frequencies, amplitudes, cellular localization and they were defined as «Ca 2C signature». 4 These Ca 2C signatures have been proven to encode a first layer of response specificity through their spatio-temporal properties. 3,5 A second layer of specificity is brought by the decoding processes requiring calcium-binding proteins also referred as calcium sensors and their downstream targets. Ca 2C sensors are characterized by the presence in their sequence of the canonical Ca 2C -binding motif called EF-hand. 6 The Arabidopsis genome encodes at least 250 EF-hand proteins, which is much higher than in mammals, arguing for higher importance of this class of proteins in plants. 7 These Ca 2C sensors are classified into 4 major groups, the calcineurin-B like, the calciumdependent kinases, the calmodulin group and a closely related group, the CalModulin-Like protein (CML) family, which is specific to plants. 8 In 2017, we reported that the ectopic CML8 expression (P35S:: cds CML8) confers to transgenic plants a ...

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Evolution of the EF-Hand Family of Proteins

Cited by 192 publications

References 4 publications

Six Arabidopsis thaliana homologues of the human respiratory burst oxidase (gp91^phox)

Six Arabidopsis thaliana homologues of the human respiratory burst oxidase (gp91^phox)

Characterization and Immunolocalization of a Cytosolic Calcium-Binding Protein from Brassica napus and Arabidopsis Pollen1

Respective contribution of CML8 and CML9, two arabidopsis calmodulin-like proteins, to plant stress responses

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Evolution of the EF-Hand Family of Proteins

Cited by 192 publications

References 4 publications

Six Arabidopsis thaliana homologues of the human respiratory burst oxidase (gp91phox)

Six Arabidopsis thaliana homologues of the human respiratory burst oxidase (gp91phox)

Characterization and Immunolocalization of a Cytosolic Calcium-Binding Protein from Brassica napus and Arabidopsis Pollen1

Respective contribution of CML8 and CML9, two arabidopsis calmodulin-like proteins, to plant stress responses

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Six Arabidopsis thaliana homologues of the human respiratory burst oxidase (gp91^phox)

Six Arabidopsis thaliana homologues of the human respiratory burst oxidase (gp91^phox)