Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Pubmed ID :20658158
Publication Date : //

Enzymes of cysteine synthesis show extensive and conserved modifications patterns that include N(α)-terminal acetylation.

Biosynthesis of cysteine is a two-step process in higher plants subsequently catalyzed by serine acetyltransferase (SAT) and O-acetylserine (thiol) lyase (OAS-TL) which are present in cytosol, plastids and mitochondria. Recently, the distribution of SAT and OAS-TL in these subcellular compartments was shown to be crucial for efficient cysteine synthesis in Arabidopsis thaliana. In this study, the abundances of OAS-TLs were quantified independently by immunological detection in crude protein extracts and by SAT affinity purification (SAP) of OAS-TL. OAS-TL A and B were evidenced to be the most abundant isoforms in all analyzed tissues, which is consistent with micro array-based transcript analyses. Application of SAP to Arabidopsis revealed significant modification of the major OAS-TL isoforms present in cytosol, plastids and mitochondria into up to seven subspecies. Specific OAS-TL isoforms were found to be differentially modified in the leaves, roots, stem and cell culture. Sulphur deficiency did not alter modification of OAS-TL proteins purified from cell culture that showed the highest complexity of OAS-TL modifications. However, the pattern of OAS-TL modification was found to be stable within an analyzed tissue, pointing not only to a high reproducibility of SAP but likely biological significance of each subspecies. The most abundant OAS-TL subspecies in cytosol and plastids were subject of N-terminal processing followed by acetylation of the newly originated N-terminus. The mode of N(α)-terminal acetylation of OAS-TL and its possible biological function are discussed.

Authors : Wirtz Markus , Heeg Corinna , Samami Arman Allboje , Ruppert Thomas , Hell Rüdiger ,

Related products :

Catalog number Product name Quantity
26-327 N-alpha-acetylation is one of the most common protein modifications that occurs during protein synthesis and involves the transfer of an acetyl group from acetyl-coenzyme A to the protein alpha-amino 0.05 mg
27-212 WDR3 is a nuclear protein containing 10 WD repeats. WD repeats are approximately 30- to 40-amino acid domains containing several conserved residues, which usually include a trp-asp at the C-terminal e 0.05 mg
29-894 IRF6 is a member of the interferon regulatory transcription factor (IRF) family. Family members share a highly-conserved N-terminal helix-turn-helix DNA-binding domain and a less conserved C-terminal 0.1 mg
26-174 ICMT is the third of three enzymes that posttranslationally modify isoprenylated C-terminal cysteine residues in certain proteins and target those proteins to the cell membrane. This enzyme localizes 0.05 mg
25-876 Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, 0.05 mg
27-181 PNPO catalyzes the terminal, rate-limiting step in the synthesis of pyridoxal 5'-phosphate, also known as vitamin B6. Vitamin B6 is a required co-factor for enzymes involved in both homocysteine metab 0.05 mg
29-938 SLC26A1 is a member of sulfate_anion transporter family. Family members are well conserved in their protein (aa length among species) structures, but have markedly different tissue expression patterns 0.05 mg
26-488 N-glycosylation of proteins follows a highly conserved pathway that begins with the synthesis of a 0.05 mg
30-588 N-glycosylation of proteins follows a highly conserved pathway that begins with the synthesis of a 0.05 mg
AS03 034 Antibody: Cyt b6 | thylakoid membrane cytochrome b6 protein, N terminal, Immunogen: KLH-conjugated peptide chosen from N terminal sequence of cytb6 conserved in Arabidopsis thaliana P56773 and Chlamyd 100
28-521 ANXA11 is a member of the annexin family, a group of calcium-dependent phospholipid-binding proteins. Annexins have unique N-terminal domains and conserved C-terminal domains, which contain the calciu 0.1 mg
25-739 STC1 is a secreted, homodimeric glycoprotein that is expressed in a wide variety of tissues and may have autocrine or paracrine functions. It contains 11 conserved cysteine residues and is phosphoryla 0.05 mg
32-162 Granulins are a family of secreted, glycosylated peptides that are cleaved from a single precursor protein with 7.5 repeats of a highly conserved 12-cysteine granulin_epithelin motif. The 88 kDa precu 0.1 mL
28-920 Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. SAP18 is a component of the histone 0.05 mg
28-857 Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. SAP30 is a component of the histone 0.1 mg
28-858 Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. SAP30 is a component of the histone 0.1 mg
orb82797 Mouse FGF7 protein Fibroblast Growth Factor-7 (FGF-7_KGF) is one of 23 known members of the FGF family. All FGFs have two conserved cysteine residues and share 30 - 50 percent sequence identity at th 1 mg
29-540 FZD7 is 7-transmembrane domain protein that is receptor for Wnt signaling proteins. The FZD7 protein contains an N-terminal signal sequence, 10 cysteine residues typical of the cysteine-rich extracell 0.05 mg
enz-449 Recombinant Human Cysteine Dioxygenase ENZYMES 1mg
enz-449 Recombinant Human Cysteine Dioxygenase ENZYMES 50
enz-449 Recombinant Human Cysteine Dioxygenase ENZYMES 10
25-969 FAM19A3 is a member of the TAFA family which is composed of five highly homologous small secreted proteins. These proteins contain conserved cysteine residues at fixed positions, and are distantly rel 0.05 mg
26-623 CHCHD4, a component of human mitochondria, belongs to a protein family whose members share 6 highly conserved cysteine residues constituting a -CXC-CX (9)C-CX (9)C- motif in the C terminus.CHCHD4, a c 0.05 mg
enz-650 Recombinant Human Molybdenum Cofactor Synthesis 2 ENZYMES 100
enz-650 Recombinant Human Molybdenum Cofactor Synthesis 2 ENZYMES 2


GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur

Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur



9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017


france@gentaur.com | Gentaur

Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123

GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U

spain@gentaur.com | Gentaur

ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636

GENTAUR Poland Sp. z o.o.

ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556


Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur