PMID- 10375640
OWN - NLM
STAT- MEDLINE
DCOM- 19990805
LR  - 20190707
IS  - 0378-1119 (Print)
IS  - 0378-1119 (Linking)
VI  - 233
IP  - 1-2
DP  - 1999 Jun 11
TI  - Identification, expression and chromosome localization of a human gene encoding a
      novel protein with similarity to the pilB family of transcriptional factors
      (pilin) and to bacterial peptide methionine sulfoxide reductases.
PG  - 233-40
AB  - Here we report the isolation, characterization and chromosome localization of a
      subtracted cDNA (CBS-1) isolated from the human ocular ciliary body which encodes
      a novel protein. As is deduced from the nucleotide sequence of the cDNA, CBS-1
      contains an open reading frame consisting of 182 amino acids, with a molecular
      weight of 19.5kDa. CBS-1 shares significant nucleotide and amino acid sequence
      identities (residues 51 to 182) with a hypothetical 15.5kDa protein in the
      ANSA-GAP intergenic region (yeaA) of Escherichia coli, and the carboxyl terminal 
      region of pilB, a transcription factor involved in the regulation of expression
      of pili, from Neisseria gonorrhoeae. Interestingly, CBS-1 also shares significant
      identity with the carboxyl terminus of the peptide-methionine sulfoxide reductase
      (MsrA), a repair enzyme, from Helicobacter pylori and Streptococcus pneumoniae.
      However, the amino terminal of CBS-1 (residues 23 to 43), which lacks homology to
      the amino terminal region of gonococcal pilB or pneumococcal MsrA, exhibits
      significant identity in a stretch of 20 amino acids, with glycine-rich proteins. 
      By Northern blot, CBS-1, hybridized to a 0.6 to 0.7kb transcript in size, is
      expressed ubiquitously in many tissues, but most abundantly in the retina and
      ocular ciliary body, skeletal muscle and heart. An epitope-directed antibody to
      an amino acid sequence at the carboxyl terminus of CBS-1 recognized a main
      protein of 19.5kDa in ocular ciliary body extracts, and a 23kDa protein in total 
      extracts from E. coli MC1061 cells, which expresses high levels of MsrA. The
      CBS-1 gene was mapped to human chromosome 10p12 between markers WI-8535 and
      WI-4724, and is tightly linked to the two STRP markers of D10S1789 and D10S550.
      We suggest that the CBS-1 gene encodes a mammalian transcription factor related
      to the bacterial pilB and certain bacterial MsrA homologues.
FAU - Huang, W
AU  - Huang W
AD  - Department of Ophthalmology and Visual Science, Yale University School of
      Medicine, New Haven, CT 06510, USA.
FAU - Escribano, J
AU  - Escribano J
FAU - Sarfarazi, M
AU  - Sarfarazi M
FAU - Coca-Prados, M
AU  - Coca-Prados M
LA  - eng
SI  - GENBANK/AF122004
GR  - EY-00785/EY/NEI NIH HHS/United States
GR  - EY-04873/EY/NEI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - Netherlands
TA  - Gene
JT  - Gene
JID - 7706761
RN  - 0 (Bacterial Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (Transcription Factors)
RN  - EC 1.- (Oxidoreductases)
RN  - EC 1.8.4.- (MSRB2 protein, human)
RN  - EC 1.8.4.- (Methionine Sulfoxide Reductases)
RN  - EC 1.8.4.11 (methionine sulfoxide reductase)
RN  - EC 1.8.4.13 (pilB protein, Bacteria)
SB  - IM
MH  - Amino Acid Sequence
MH  - Bacterial Proteins/*genetics
MH  - Base Sequence
MH  - Chromosome Mapping
MH  - *Chromosomes, Human, Pair 10
MH  - Ciliary Body/enzymology
MH  - DNA, Complementary
MH  - Fluorescent Antibody Technique, Indirect
MH  - Helicobacter pylori/enzymology
MH  - Humans
MH  - Methionine Sulfoxide Reductases
MH  - Molecular Sequence Data
MH  - Oxidoreductases/*genetics
MH  - Phylogeny
MH  - Sequence Homology, Amino Acid
MH  - Streptococcus pneumoniae/enzymology
MH  - Transcription Factors/*genetics
EDAT- 1999/06/22 00:00
MHDA- 1999/06/22 00:01
CRDT- 1999/06/22 00:00
PHST- 1999/06/22 00:00 [pubmed]
PHST- 1999/06/22 00:01 [medline]
PHST- 1999/06/22 00:00 [entrez]
AID - S0378111999001316 [pii]
AID - 10.1016/s0378-1119(99)00131-6 [doi]
PST - ppublish
SO  - Gene. 1999 Jun 11;233(1-2):233-40. doi: 10.1016/s0378-1119(99)00131-6.