ライフサイエンスコーパス: BCCP

1 is complex was also formed between BPL and a BCCP Delta 67 mutant lacking the lysine residue (BCCP De

2 jacent to the biotinoyl domain resulted in a BCCP species that was defective in function in vivo, alt

3 We now report that a BCCP-87 species to which the biotin moiety was attached

4 by at least two genes, but the most abundant BCCP transcript so far has not been characterized.

5 otin transfer to the minimal biotin acceptor BCCP fragments of the carboxylases.

6 We conclude the BADC proteins are ancestral BCCPs that gained a new function as negative regulators

7 arent values for ATP, acetyl-coenzyme A, and BCCP were estimated to be 60+/-14 microM, 18+/-4 microM,

8 bunit, formed by residues between the BC and BCCP domains, is crucial for interactions with the beta-

9 or native PAGE, CT separates from the BC and BCCP subunits of plastidial-ACCase and ACCase activity i

10 Although the structures of the BC, CT and BCCP domains and other biotin-dependent carboxylase holo

11 ining the BC and the beta subunit the CT and BCCP domains, and it is believed that the holoenzyme has

12 Apo-BCCP interacts specifically with the biotin holoenzyme s

13 ide (EDC) allowed the isolation of a BPL:apo-BCCP Delta 67 complex.

14 In the absence of apo-BCCP, biotin-5'-AMP acts as a co-repressor that induces

15 Both Arabidopsis BCCP isoforms were expressed in Escherichia coli and fou

16 t and characterize here a second Arabidopsis BCCP (AtBCCP2) cDNA with 42% amino acid identity to AtBC

17 of AccA, AccD, AccC, and AccB (also known as BCCP), which is required for fatty acid biosynthesis.

18 Translation products from cDNAs for BC, BCCP, and alpha-CT were imported into isolated pea (Pisu

19 Whereas BC, BCCP, and alpha-CT are products of nuclear genes, the DN

20 interaction of BCCP with BC and that the BC.BCCP complex is a substrate for biotinylation in vitro.

21 We report isolation of the BC.BCCP complex.

22 mbinant BPL and the biotinyl domain of BCCP (BCCP Delta 67) from the extreme hyperthermophile Aquifex

23 n interactions involved are unclear as a BPL:BCCP complex has not yet been isolated.

24 specific lysine residue of each carboxylase BCCP domain.

25 coli pyruvate dehydrogenase gave a chimeric BCCP species that had normal in vivo function.

26 E. coli BCCP is a member of a large family of protein domains mo

27 In E. coli BCCP, this putative linker extends for about 42 residues

28 In contrast, replacement of the deleted BCCP linker with a linker derived from E. coli pyruvate

29 In protein blots, four different BCCP isoforms were detected in developing seeds from oil

30 oybean seeds that encode BC, two that encode BCCP, and four that encode alpha-CT.

31 uction appears closely matched to endogenous BCCP levels, since overexpression of BCCP2 produced most

32 proximately 55 A, indicating that the entire BCCP domain must translocate during catalysis.

33 sites are separated by 80 A, and the entire BCCP domain must translocate during catalysis.

34 nclude two plasmids (pTrc.BCCP and pTrc.EZZ::BCCP) which encode different 'tags' for the capture of a

35 ket) was cloned into pTrc.BCCP and pTrc.EZZ::BCCP, while the 13S E1a gene was cloned into lambdaFJG2.

36 complex consists of a dimer of BC plus four BCCP molecules instead of the 2BC.2BCCP complex previous

37 Holo-BCCP then interacts with the biotin carboxylase subunit,

38 to trypsin digestion than the wild type holo-BCCP-87.

39 ormation was considerably reduced using holo-BCCP Delta 67.

40 n that has been termed "protruding thumb" in BCCP.

41 Of these, a 35-kD BCCP was detected in immature leaves and developing seed

42 perature-sensitive E. coli strain that lacks BCCP when grown at nonpermissive temperatures.

43 to a class of oilseed rape (Brassica napus) BCCPs.

44 otin prosthetic group reduces the ability of BCCP Delta 67 to heterodimerize with BPL, and emphasizes

45 d recombinant BPL and the biotinyl domain of BCCP (BCCP Delta 67) from the extreme hyperthermophile A

46 With the exception of BCCP, single-copy genes encode these subunits in Arabido

47 Finally, the carboxybiotinylated form of BCCP interacts with transcarboxylase in the conversion o

48 an 87 residue C-terminal domain fragment of BCCP (apoBCCP87) from Escherichia coli acetyl-CoA carbox

49 BCCP are responsible for the interaction of BCCP with BC and that the BC.BCCP complex is a substrate

50 is is that posttranslational modification of BCCP may result in conformational changes that regulate

51 ort that the N-terminal 30 or so residues of BCCP are responsible for the interaction of BCCP with BC

52 Expression of BCCPs having deletions of various segments of the linker

53 BPL catalyses biotinylation of lysine 117 on BCCP Delta 67 at temperatures of up to 70 degrees C.

54 of biotin to an essential lysine residue on BCCP.

55 iological significance of the two paralogous BCCP-coding genes, CAC1A (At5g16390, codes for BCCP1) an

56 0.5 M KCl, a complex that contained BC plus BCCP emerged from Sephacryl 400 with an apparent molecul

57 cies of the biotin carboxyl carrier protein (BCCP) biotinoyl domain is much more resistant to chemica

58 se (CT) and biotin carboxyl carrier protein (BCCP) components.

59 otin to the biotin carboxyl carrier protein (BCCP) domain of five biotin-dependent carboxylases.

60 se (BC) and biotin carboxyl carrier protein (BCCP) domains, whereas the beta-subunit supplies the car

61 Biotin carboxyl carrier protein (BCCP) in Arabidopsis is encoded by at least two genes, b

62 The biotin carboxyl carrier protein (BCCP) is a subunit of acetyl-CoA carboxylase, a biotin-d

63 Biotin carboxyl carrier protein (BCCP) is the small biotinylated subunit of Escherichia c

64 ith the two biotin carboxyl carrier protein (BCCP) isoforms of A. thaliana ACCase.

65 idue of the biotin carboxyl carrier protein (BCCP) of acetyl CoA carboxylase.

66 that of the biotin carboxyl carrier protein (BCCP) of acetyl-CoA carboxylase, but lacks an extension

67 tion of the biotin carboxyl carrier protein (BCCP) subunit of acetyl CoA carboxylase and this post-tr

68 se (BC) and biotin carboxyl carrier protein (BCCP) subunits have been reported in the literature, but

69 s of the biotin carboxylase carrier protein (BCCP) under the control of the Ptac promoter, while the

70 ylase (BC), biotin carboxyl carrier protein (BCCP), and beta-carboxyltransferase (CT) subunits of the

71 ylase (BC), biotin carboxyl carrier protein (BCCP), and the alpha- and beta-subunits of carboxyltrans

72 r subunits: biotin carboxyl-carrier protein (BCCP), biotin carboxylase, alpha-carboxyltransferase, an

73 he acceptor biotin carboxyl carrier protein (BCCP), through the expected biotinoyl-AMP intermediate.

74 bunits, the biotin carboxyl carrier protein (BCCP), was previously proposed to be encoded by a single

75 otin to the biotin carboxyl carrier protein (BCCP).

76 ntly to the biotin carboxyl carrier protein (BCCP).

77 n of E.coli biotin carboxyl carrier protein (BCCP).

78 ylase (BC), biotin-carboxyl carrier protien (BCCP), and carboxytransferase (alpha-CT, beta-CT) subuni

79 the E1A-binding pocket) was cloned into pTrc.BCCP and pTrc.EZZ::BCCP, while the 13S E1a gene was clon

80 The first plasmid (pTrc.BCCP) encodes the C terminus of the biotin carboxylase c

81 The vectors include two plasmids (pTrc.BCCP and pTrc.EZZ::BCCP) which encode different 'tags' f

82 tain at least one to three seed-up-regulated BCCP isoforms, depending upon genome complexity.

83 These proteins resemble BCCP subunits but are not biotinylated due to a mutated

84 Delta 67 mutant lacking the lysine residue (BCCP Delta 67 K117L) however, complex formation was cons

85 The BCCP domain is located in the active site of the beta-su

86 esults demonstrate that biotinylation of the BCCP fragments of the mitochondrial carboxylases propion

87 ved structure of the biotinoyl domain of the BCCP subunit is disrupted by a structured loop called th

88 These BCCP species were produced in both the apo and holo form

89 Expression of this BCCP species failed to restore normal growth and fatty a

90 in transfer of biotin from the adenylate to BCCP.

91 was shown that the complex consists of a two BCCP molecules per BC molecule.

92 er holo form stability by examination of two BCCP-87 species that lack the thumb.

93 Deletions within the linker of the wild type BCCP protein also showed that the residues adjacent to t

94 e coupled activities of AccC and AccA/D with BCCP cycling between the two half-reactions.