scholarly journals GhYGL1d, a pentatricopeptide repeat protein, is required for chloroplast development in cotton

2019 ◽  
Author(s):  
Peng He ◽  
Shuyin Wu ◽  
Yanli Jiang ◽  
Lihua Zhang ◽  
Meiju Tang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Gene Families ◽  
Wild Type ◽  
Pentatricopeptide Repeat ◽  
Amino Acid Sequence Homology ◽  
Plastid Development ◽  
Amino Acid Repeats ◽  
Leaf Variegation ◽  
High Amino Acid ◽  
Ppr Proteins

Abstract Background: The pentatricopeptide repeat (PPR) gene family, which contains multiple 35-amino acid repeats, constitutes one of the largest gene families in plants. PPR proteins function in organelles to target specific transcripts and are involved in plant development and growth. However, the function of PPR proteins in cotton is still unknown. Results: In this study, we characterized a PPR gene YELLOW-GREEN LEAF (GhYGL1d) that is required for cotton plastid development. The GhYGL1d gene has a DYW domain in C-terminal and is highly express in leaves, localized to the chloroplast fractions. GhYGL1d share high amino acid-sequence homology with AtECB2. In atecb2 mutant, overexpression of GhYGL1d rescued the seedling lethal phenotype and restored the editing of accD and ndhF transcripts. Silencing of GhYGL1d led to the reduction of chlorophyll and phenotypically yellow-green leaves in cotton. Compared with wild type, GhYGL1d-silenced cotton showed significant deformations of thylakoid structures. Furthermore, the transcription levels of plastid-encoded polymerase (PEP) and nuclear-encoded polymerase (NEP) dependent genes were decreased in GhYGL1d-silenced cotton. Conclusions: Our data indicate that GhYGL1d not only contributes to the editing of accD and ndhF genes, but also affects the expression of NEP- and PEP-dependent genes to regulate the development of thylakoids, and therefore regulates leaf variegation in cotton.

scholarly journals GhYGL1d, a pentatricopeptide repeat protein, is required for chloroplast development in cotton

2019 ◽  
Author(s):  
Peng He ◽  
Shuyin Wu ◽  
Yanli Jiang ◽  
Lihua Zhang ◽  
Meiju Tang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Gene Families ◽  
Wild Type ◽  
Pentatricopeptide Repeat ◽  
Amino Acid Sequence Homology ◽  
Plastid Development ◽  
Amino Acid Repeats ◽  
Leaf Variegation ◽  
High Amino Acid ◽  
Ppr Proteins

Abstract Background: The pentatricopeptide repeat (PPR) gene family, which contains multiple 35-amino acid repeats, constitutes one of the largest gene families in plants. PPR proteins function in organelles to target specific transcripts and are involved in plant development and growth. However, the function of PPR proteins in cotton is still unknown. Results: In this study, we characterized a PPR gene YELLOW-GREEN LEAF (GhYGL1d) that is required for cotton plastid development. The GhYGL1d gene has a DYW domain in C-terminal and is highly express in leaves, localized to the chloroplast fractions. GhYGL1d share high amino acid-sequence homology with AtECB2. In atecb2 mutant, overexpression of GhYGL1d rescued the seedling lethal phenotype and restored the editing of accD and ndhF transcripts. Silencing of GhYGL1d led to the reduction of chlorophyll and phenotypically yellow-green leaves in cotton. Compared with wild type, GhYGL1d-silenced cotton showed significant deformations of thylakoid structures. Furthermore, the transcription levels of plastid-encoded polymerase (PEP) and nuclear-encoded polymerase (NEP) dependent genes were decreased in GhYGL1d-silenced cotton. Conclusions: Our data indicate that GhYGL1d not only contributes to the editing of accD and ndhF genes, but also affects the expression of NEP- and PEP-dependent genes to regulate the development of thylakoids, and therefore regulates leaf variegation in cotton.

scholarly journals GhYGL1d, a pentatricopeptide repeat protein, is required for chloroplast development in cotton

2019 ◽  
Author(s):  
Peng He ◽  
Shuyin Wu ◽  
Yanli Jiang ◽  
Lihua Zhang ◽  
Meiju Tang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Gene Families ◽  
Wild Type ◽  
Pentatricopeptide Repeat ◽  
Amino Acid Sequence Homology ◽  
Plastid Development ◽  
Amino Acid Repeats ◽  
Leaf Variegation ◽  
High Amino Acid ◽  
Ppr Proteins

Abstract Background: The pentatricopeptide repeat (PPR) gene family, which contains multiple 35-amino acid repeats, constitutes one of the largest gene families in plants. PPR proteins function in organelles to target specific transcripts and are involved in plant development and growth. However, the function of PPR proteins in cotton is still unknown. Results: In this study, we characterized a PPR gene YELLOW-GREEN LEAF (GhYGL1d) that is required for cotton plastid development. The GhYGL1d gene has a DYW domain in C-terminal and is highly express in leaves, localized to the chloroplast fractions. GhYGL1d share high amino acid-sequence homology with AtECB2. In atecb2 mutant, overexpression of GhYGL1d rescued the seedling lethal phenotype and restored the editing of accD and ndhF transcripts. Silencing of GhYGL1d led to the reduction of chlorophyll and phenotypically yellow-green leaves in cotton. Compared with wild type, GhYGL1d-silenced cotton showed significant deformations of thylakoid structures. Furthermore, the transcription levels of plastid-encoded polymerase (PEP) and nuclear-encoded polymerase (NEP) dependent genes were decreased in GhYGL1d-silenced cotton. Conclusions: Our data indicate that GhYGL1d not only contributes to the editing of accD and ndhF genes, but also affects the expression of NEP- and PEP-dependent genes to regulate the development of thylakoids, and therefore regulates leaf variegation in cotton.

scholarly journals GhYGL1, a pentatricopeptide repeat protein, is required for chloroplast development in cotton

2019 ◽  
Author(s):  
Peng He ◽  
Shuyin Wu ◽  
Yanli Jiang ◽  
Lihua Zhang ◽  
Meiju Tang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Gene Families ◽  
Pentatricopeptide Repeat ◽  
Amino Acid Sequence Homology ◽  
Plastid Development ◽  
Amino Acid Repeats ◽  
Leaf Variegation ◽  
Leaf Phenotype ◽  
High Amino Acid ◽  
Ppr Genes

Abstract Background The pentatricopeptide repeat (PPR) gene family, which contains multiple 35-amino acid repeats, constitutes one of the largest gene families in plants. Pentatricopeptide repeat genes function in organelles to target specific transcripts and are involved in plant development and growth. However, the function of PPR genes in cotton is still unknown. Results In this study, we characterized a PPR gene (GhYGL1), producing a yellow green leaf phenotype, that is required for cotton plastid development. The GhYGL1 gene has a DYW domain in C-terminal and is highly express in leaves, localized to the chloroplast fractions. GhYGL1 share high amino acid-sequence homology with AtECB2. In ecb2-mutated Arabidopsis, overexpression of GhYGL1 rescued the seedling lethal phenotype and restored the editing of accD and ndhF transcripts. Silencing of GhYGL1 led to the reduction of chlorophyll and phenotypically yellow-green leaves in cotton. Compared with wild type, GhYGL1-silenced cotton showed significant deformations of thylakoid structures. Furthermore, the expression levels of plastid-encoded polymerase- (PEP) and nuclear-encoded polymerase- (NEP) dependent genes were significantly decreased in GhYGL1-silenced cotton. Conclusions Our data indicate that GhYGL1 not only controls the editing of accD and ndhF genes, but also controls the expression of NEP- and PEP-dependent genes to regulate the development of thylakoids, and therefore regulates leaf variegation in cotton.

scholarly journals A Ubiquitin-Conjugating Enzyme Is Essential for Developmental Transitions in Dictyostelium

1997 ◽  
Vol 8 (10) ◽  
pp. 1989-2002 ◽  
Author(s):  
Alexandra Clark ◽  
Anson Nomura ◽  
Sudhasri Mohanty ◽  
Richard A. Firtel
Keyword(s):  
Gene Expression ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Specific Gene ◽  
Wild Type ◽  
Cell Type ◽  
Protein Ubiquitination ◽  
High Amino Acid ◽  
Cell Type Specific ◽  
Very High

We have identified a developmentally essential gene,UbcB, by insertional mutagenesis. The encoded protein (UBC1) shows very high amino acid sequence identity to ubiquitin-conjugating enzymes from other organisms, suggesting that UBC1 is involved in protein ubiquitination and possibly degradation during Dictyostelium development. Consistent with the homology of the UBC1 protein to UBCs, the developmental pattern of protein ubiquitination is altered in ubcB-null cells.ubcB-null cells are blocked in the ability to properly execute the developmental transition that occurs between the induction of postaggregative gene expression during mound formation and the induction of cell-type differentiation and subsequent morphogenesis.ubcB-null cells plated on agar form mounds with normal kinetics; however, they remain at this stage for ∼10 h before forming multiple tips and fingers that then arrest. Under other conditions, some of the fingers form migrating slugs, but no culmination is observed. In ubcB-null cells, postaggregative gene transcripts accumulate to very high levels and do not decrease significantly with time as they do in wild-type cells. Expression of cell-type-specific genes is very delayed, with the level of prespore-specific gene expression being significantly reduced compared with that in wild-type cells. lacZ reporter studies using developmentally regulated and cell-type-specific promoters suggest that ubcB-null cells show an unusually elevated level of staining of lacZ reporters expressed in anterior-like cells, a regulatory cell population found scattered throughout the aggregate, and reduced staining of a prespore reporter.ubcB-null cells in a chimeric organism containing predominantly wild-type cells are able to undergo terminal differentiation but show altered spatial localization. In contrast, in chimeras containing only a small fraction of wild-type cells, the mature fruiting body is very small and composed almost exclusively of wild-type cells, with the ubcB-null cells being present as a mass of cells located in extreme posterior of the developing organism. The amino acid sequence analysis of the UbcBopen reading frame (ORF) and the analysis of the developmental phenotypes suggest that tip formation and subsequent development requires specific protein ubiquitination, and possibly degradation.

scholarly journals The Nature and Arrangement of Pentatricopeptide Domains and the Linker Sequences Between Them

2020 ◽  
Vol 14 ◽  
pp. 117793222090643 ◽  
Author(s):  
Sailen Barik
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Function ◽  
Bioinformatic Analysis ◽  
Acid Number ◽  
Tetratricopeptide Repeat ◽  
Pentatricopeptide Repeat ◽  
Alpha Helices ◽  
Common Amino Acid ◽  
Amino Acid Repeats

The tricopeptide (amino acid number in the 30s) repeats constitute some of the most common amino acid repeats in proteins of diverse organisms. The most important representatives of this class are the 34-residue and 35-residue repeats, eponymously known as tetratricopeptide repeat (TPR) and pentatricopeptide repeat (PPR), respectively. The unit motif of both consists of a pair of alpha helices. As members of the large, all-helical repeat classes, TPR and PPR share structural similarities, but also play specific roles in protein function. In this study, a comprehensive bioinformatic analysis of the PPR units and the linkers that connect them was conducted. The results suggested the existence of PPR repeats of various formats, as well as smaller, PPR-unrelated repeats. Besides their length, these repeats differed in amino acid arrangements and location of key amino acids. These findings provide a broader and unified perspective of the pentatricopeptide family while raising provocative questions about the assembly and evolution of these domains.

The rice cytosolic pentatricopeptide repeat protein OsPPR2-1 regulates OsGLK1 to control tapetal plastid development and programmed cell death

2021 ◽  
Author(s):  
Shaoyan Zheng ◽  
Jingfang Dong ◽  
Jingqin Lu ◽  
Jing Li ◽  
Dagang Jiang ◽  
...  
Keyword(s):  
Cell Death ◽  
Programmed Cell Death ◽  
Pollen Fertility ◽  
Oryza Sativa L ◽  
Pentatricopeptide Repeat ◽  
Plastid Development ◽  
Mobility Shift ◽  
Ppr Protein ◽  
Ppr Proteins

Abstract Most pentatricopeptide repeat (PPR) proteins localize to plastids or mitochondria, where they participate in RNA metabolism and post-transcriptionally regulate organelle gene expression. However, whether PPR proteins regulate the expression of nucleus-encoded genes remains unclear. Here, we uncovered a function for the rice (Oryza. sativa L.) PPR protein OsPPR2-1 (Os02g0110400) in pollen development and showed that, in contrast to most other PPR proteins, OPPR2-1 resides in the cytoplasm. Downregulating OsPPR2-1 expression led to abnormal plastid development in tapetal cells, prolonged programmed cell death (PCD), prolonged tapetum degradation, and significantly reduced pollen fertility. Transcriptome analysis revealed that the expression of OsGOLDEN-LIKE 1 (OsGLK1), encoding a transcription factor that regulates plastid development and maintenance, was significantly higher in plants with downregulated OsPPR2-1 expression compared to the wild type. Moreover, OsPPR2-1 bound to the OsGLK1 mRNA in RNA immunoprecipitation and RNA-electrophoretic mobility shift assays. An in vitro cleavage assay showed that OsPPR2-1 could degrade the OsGLK1 mRNA. Notably, knockdown of OsGLK1 partially restored pollen fertility in OsPPR2-1-knockdown plants and OsGLK1-overexpressing plants showed abnormal tapetum and plastid development, similar to the OsPPR2-1-knockdown plants. Together, our findings demonstrate that OsPPR2-1 regulates OsGLK1 expression, thereby controlling plastid development and PCD in the tapetum.

scholarly journals OsPPR939, a nad5 splicing factor, is essential for plant growth and pollen development in rice

2021 ◽  
Author(s):  
Peng Zheng ◽  
Yujun Liu ◽  
Xuejiao Liu ◽  
Yuqing Huang ◽  
Feng Sun ◽  
...  
Keyword(s):  
Amino Acid ◽  
Plant Growth ◽  
Pollen Development ◽  
Phosphorylation Site ◽  
Plant Morphology ◽  
Pentatricopeptide Repeat ◽  
Respiratory Pathway ◽  
Ppr Protein ◽  
Ppr Proteins ◽  
Splicing Efficiency

Abstract Key message P-subfamily PPR protein OsPPR939, which can be phosphorylated by OsS6K1, regulates plant growth and pollen development by involving in the splicing of mitochondrial nad5 introns 1, 2, and 3. Abstract In land plants, pentatricopeptide repeat (PPR) proteins play key roles in mitochondrial group II intron splicing, but how these nucleus-encoded proteins are imported into mitochondria is unknown. To date, a few PPR proteins have been characterized in rice (Oryza sativa). Here, we demonstrate that the mitochondrion-localized P-subfamily PPR protein OsPPR939 is required for the splicing of nad5 introns 1, 2, and 3 in rice. Complete knockout or partial disruption of OsPPR939 function resulted in different degrees of growth retardation and pollen sterility. The dramatically reduced splicing efficiency of these introns in osppr939-4 and osppr939-5 led to reduced mitochondrial complex I abundance and activity and enhanced expression of alternative respiratory pathway genes. Complementation with OsPPR939 rescued the defective plant morphology of osppr939-4 and restored its decreased splicing efficiency of nad5 introns 1, 2, and 3. Therefore, OsPPR939 plays crucial roles in plant growth and pollen development by splicing mitochondrial nad5 introns 1, 2, and 3. More importantly, the 12th amino acid Ser in the N-terminal targeting sequence of OsPPR939 is phosphorylated by OsS6K1, and truncated OsPPR939 with a non-phosphorylatable S12A mutation in its presequence could not be imported into mitochondria, suggesting that phosphorylation of this amino acid plays an important role in the mitochondrial import of OsPPR939. To our knowledge, the 12th residue Ser on OsPPR939 is the first experimentally proven phosphorylation site in PPR proteins. Our results provide a basis for investigating the regulatory mechanism of PPR proteins at the post-translational level.

Recombinant Variants of Tissue-Type Plasminogen Activator Containing Amino Acid Substitutions in the Finger Domain

1992 ◽  
Vol 68 (06) ◽  
pp. 672-677 ◽  
Author(s):  
Hitoshi Yahara ◽  
Keiji Matsumoto ◽  
Hiroyuki Maruyama ◽  
Tetsuya Nagaoka ◽  
Yasuhiro Ikenaka ◽  
...  
Keyword(s):  
Amino Acid ◽  
Plasminogen Activator ◽  
Half Life ◽  
Tissue Type ◽  
Clot Lysis ◽  
Amino Acid Substitutions ◽  
Wild Type ◽  
Plasma Clot ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator

SummaryTissue-type plasminogen activator (t-PA) is a fibrin-specific agent which has been used to treat acute myocardial infarction. In an attempt to clarify the determinants for its rapid clearance in vivo and high affinity for fibrin clots, we produced five variants containing amino acid substitutions in the finger domain, at amino acid residues 7–9, 10–14, 15–19, 28–33, and 37–42. All the variants had a prolonged half-life and a decreased affinity for fibrin of various degrees. The 37–42 variant demonstrated about a 6-fold longer half-life with a lower affinity for fibrin. Human plasma clot lysis assay estimated the fibrinolytic activity of the 37–42 variant to be 1.4-fold less effective than that of the wild-type rt-PA. In a rabbit jugular vein clot lysis model, doses of 1.0 and 0.15 mg/kg were required for about 70% lysis in the wild-type and 37–42 variant, respectively. Fibrinogen was degraded only when the wild-type rt-PA was administered at a dose of 1.0 mg/kg. These findings suggest that the 37–42 variant can be employed at a lower dosage and that it is a more fibrin-specific thrombolytic agent than the wild-type rt-PA.

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