New Approach to Detect Coiled Coil and Leucine Zipper Motifs in Protein Sequences

2018 ◽  
Vol 25 (11) ◽  
pp. 1278-1283
Author(s):  
Dinko Osmankovic ◽  
Semir Doric ◽  
Naris Pojskic ◽  
Lada Lukic Bilela
Keyword(s):  
Leucine Zipper ◽  
Coiled Coil ◽  
Protein Sequences ◽  
New Approach

Leucine Is the Most Stabilizing Aliphatic Amino Acid in thedPosition of a Dimeric Leucine Zipper Coiled Coil

Biochemistry ◽  
1997 ◽  
Vol 36 (41) ◽  
pp. 12567-12573 ◽  
Author(s):  
Jaideep Moitra ◽  
Lászlo Szilák ◽  
Dmitry Krylov ◽  
Charles Vinson
Keyword(s):  
Amino Acid ◽  
Leucine Zipper ◽  
Coiled Coil ◽  
Aliphatic Amino Acid

scholarly journals Leucine-zipper-mediated homo- and hetero-dimerization of GIT family p95-ARF GTPase-activating protein, PIX-, paxillin-interacting proteins 1 and 2

2003 ◽  
Vol 372 (2) ◽  
pp. 391-398 ◽  
Author(s):  
Simona PARIS ◽  
Renato LONGHI ◽  
Paolo SANTAMBROGIO ◽  
Ivan de CURTIS
Keyword(s):  
Leucine Zipper ◽  
Coiled Coil ◽  
Actin Dynamics ◽  
Exchange Factor ◽  
Gtpase Activating Proteins ◽  
Rac Gtpases ◽  
Coiled Coil Region ◽  
The Family ◽  
G Protein Coupled ◽  
Adp Ribosylation Factor

ADP-ribosylation factor GTPase-activating proteins (ARFGAPs) of the G-protein-coupled receptor kinase interactor 1/p95 paxillin kinase linker/p95-ARFGAP Pak-interacting exchange factor paxillin-binding protein (APP)-1 family are multidomain proteins, which interact functionally with both ARF and Rac GTPases. These proteins are involved in the dynamic reorganization of adhesion and the cytoskeleton during cell motility. Our previous work [Di Cesare, Paris, Albertinazzi, Dariozzi, Andersen, Mann, Longhi and de Curtis (2000) Nat. Cell Biol. 2, 521–530] has pointed out a role for p95-APP1 in the regulation of ARF6-mediated membrane recycling. These proteins include different domains, and are capable of interacting stably with proteins that are supposed to play a role in the regulation of actin dynamics and adhesion. They contain a coiled-coil region comprising a putative leucine zipper, predicted to be involved in dimerization. In the present study, we have investigated the possibility that these proteins form dimers. Our results show that p95-APP1 forms homodimers and may also form heterodimers with the other member of the family, p95 paxillin kinase linker/p95-APP2. Both homo- and heterodimerization are disrupted by mutation of two leucine residues in the coiled-coil region of p95-APP1. The N-terminal portion of p95-APP1, including the ARFGAP domain, three ankyrin repeats and the Pak-interacting exchange factor-binding region, are not required for dimerization. Evidence is presented for the existence of endogenous oligomeric complexes. The implication of dimerization/oligomerization in the functioning of these proteins is discussed.

X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil

Science ◽  
1991 ◽  
Vol 254 (5031) ◽  
pp. 539-544 ◽  
Author(s):  
E. O'Shea ◽  
J. Klemm ◽  
P. Kim ◽  
T Alber
Keyword(s):  
Leucine Zipper ◽  
Coiled Coil ◽  
X Ray

scholarly journals Characterization of a novel human sperm-associated antigen 9 (SPAG9) having structural homology with c-Jun N-terminal kinase-interacting protein

2005 ◽  
Vol 389 (1) ◽  
pp. 73-82 ◽  
Author(s):  
Nirmala JAGADISH ◽  
Ritu RANA ◽  
Ramasamy SELVI ◽  
Deepshikha MISHRA ◽  
Manoj GARG ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Leucine Zipper ◽  
Transmembrane Domain ◽  
Coiled Coil ◽  
Human Sperm ◽  
Human Spermatozoa ◽  
Structural Homology ◽  
Chromosome 11 ◽  
Interacting Protein

We report a novel SPAG9 (sperm-associated antigen 9) protein having structural homology with JNK (c-Jun N-terminal kinase)-interacting protein 3. SPAG9, a single copy gene mapped to the human chromosome 17q21.33 syntenic with location of mouse chromosome 11, was earlier shown to be expressed exclusively in testis [Shankar, Mohapatra and Suri (1998) Biochem. Biophys. Res. Commun. 243, 561–565]. The SPAG9 amino acid sequence analysis revealed identity with the JNK-binding domain and predicted coiled-coil, leucine zipper and transmembrane domains. The secondary structure analysis predicted an α-helical structure for SPAG9 that was confirmed by CD spectra. Microsequencing of higher-order aggregates of recombinant SPAG9 by tandem MS confirmed the amino acid sequence and mono atomic mass of 83.9 kDa. Transient expression of SPAG9 and its deletion mutants revealed that both leucine zipper with extended coiled-coil domains and transmembrane domain of SPAG9 were essential for dimerization and proper localization. Studies of MAPK (mitogenactivated protein kinase) interactions demonstrated that SPAG9 interacted with higher binding affinity to JNK3 and JNK2 compared with JNK1. No interaction was observed with p38α or extracellular-signal-regulated kinase pathways. Polyclonal antibodies raised against recombinant SPAG9 recognized native protein in human sperm extracts and localized specifically on the acrosomal compartment of intact human spermatozoa. Acrosome-reacted spermatozoa demonstrated SPAG9 immunofluorescence, indicating its retention on the equatorial segment after the acrosome reaction. Further, anti-SPAG9 antibodies inhibited the binding of human spermatozoa to intact human oocytes as well as to matched hemizona. This is the first report of sperm-associated JNK-binding protein that may have a role in spermatozoa–egg interaction.

scholarly journals Class II LBD genes ZmLBD5 and ZmLBD33 regulate gibberellin and abscisic acid biosynthesis

2021 ◽  
Author(s):  
Jing Xiong ◽  
Xuanjun Feng ◽  
Weixiao Zhang ◽  
Xianqiu Wang ◽  
Yue Hu ◽  
...  
Keyword(s):  
Abscisic Acid ◽  
Leucine Zipper ◽  
Stomatal Density ◽  
Coiled Coil ◽  
Dry Weight ◽  
Class Ii ◽  
Class I ◽  
Luciferase Expression ◽  
Dwarf Phenotype ◽  
Abscisic Acid Biosynthesis

Lateral organ boundaries domain (LBD) proteins are plant-specific transcription factors. Class I LBD members are widely reported to be pivotal for organ development, however, the role of class II members is unknown in cereal crops. Class II LBD proteins are distinguished from class I by the lack of a Gly-Ala-Ser (GAS) peptide and leucine-zipper-like coiled-coil domain, which is thought to be essential for protein dimerization. In this study, ZmLBD5 and ZmLBD33 form homo- and hetero-dimers, like class I members. At seedling stage, ZmLBD5 promoted biomass accumulation (shoot dry weight and root dry weight), root development (root length, root number, and root volume), and organ expansion (leaf area), while ZmLBD33 repressed these processes and display a dwarf phenotype. Both ZmLBD5 and ZmLBD33 displayed negative roles in drought tolerance mainly by increasing stomatal density and stomatal aperture. RNA sequencing, gene ontology enrichment analysis, and transient luciferase expression assays indicated that ZmLBD5 and ZmLBD33 are mainly involved in the regulation of the TPS-KS-GA2ox gene module, which comprises key enzymatic genes upstream of GA and ABA biosynthesis. GA1 content increased in ZmLBD5-overexpressing seedlings, while GA3 and abscisic acid content decreased in both transgenic seedlings. Consequently, exogenous GA1 or GA3 undoubtedly rescued the dwarf phenotype of ZmLBD33-overexpressing plants, with GA1 performing better. The study of ZmLBD5 and ZmLBD33 sheds light on the function of the class II LBD gene family in maize.

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